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Database: PDB
Entry: 5UQ2
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Original site: 5UQ2 
HEADER    TRANSFERASE/CELL CYCLE                  06-FEB-17   5UQ2              
TITLE     CRYSTAL STRUCTURE OF HUMAN CDK2-SPY1 COMPLEX                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 2;                                 
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CELL DIVISION PROTEIN KINASE 2,P33 PROTEIN KINASE;          
COMPND   5 EC: 2.7.11.22;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: SPEEDY PROTEIN A;                                          
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: UNP RESIDUES 61-213;                                       
COMPND  11 SYNONYM: RAPID INDUCER OF G2/M PROGRESSION IN OOCYTES A,HSPY/RINGO A,
COMPND  12 SPEEDY-1,SPY1;                                                       
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 OTHER_DETAILS: SPY1A ISOFORM, SPEEDY/RINGO BOX                       
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDK2, CDKN2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: SPDYA, SPDY1, SPY1;                                            
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    PHOSPHOTRANSFERASE, PROTEIN KINASE, CELL CYCLE REGULATION,            
KEYWDS   2 TRANSFERASE-CELL CYCLE COMPLEX                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.A.MCGRATH,S.M.TRIPATHI,S.M.RUBIN                                    
REVDAT   3   09-AUG-17 5UQ2    1       JRNL                                     
REVDAT   2   19-JUL-17 5UQ2    1       JRNL                                     
REVDAT   1   05-JUL-17 5UQ2    0                                                
JRNL        AUTH   D.A.MCGRATH,B.A.FIFIELD,A.H.MARCEAU,S.TRIPATHI,L.A.PORTER,   
JRNL        AUTH 2 S.M.RUBIN                                                    
JRNL        TITL   STRUCTURAL BASIS OF DIVERGENT CYCLIN-DEPENDENT KINASE        
JRNL        TITL 2 ACTIVATION BY SPY1/RINGO PROTEINS.                           
JRNL        REF    EMBO J.                       V.  36  2251 2017              
JRNL        REFN                   ESSN 1460-2075                               
JRNL        PMID   28666995                                                     
JRNL        DOI    10.15252/EMBJ.201796905                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 85.50                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 16210                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.010                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1622                            
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 85.5391 -  6.1818    1.00     1336   149  0.1949 0.2454        
REMARK   3     2  6.1818 -  4.9068    1.00     1244   139  0.2004 0.2533        
REMARK   3     3  4.9068 -  4.2866    1.00     1227   136  0.1701 0.2220        
REMARK   3     4  4.2866 -  3.8947    1.00     1207   134  0.1811 0.2431        
REMARK   3     5  3.8947 -  3.6155    0.99     1217   136  0.2008 0.2984        
REMARK   3     6  3.6155 -  3.4023    1.00     1210   133  0.2307 0.2753        
REMARK   3     7  3.4023 -  3.2319    1.00     1190   133  0.2477 0.3554        
REMARK   3     8  3.2319 -  3.0912    1.00     1198   133  0.2683 0.3278        
REMARK   3     9  3.0912 -  2.9722    1.00     1191   132  0.2601 0.3322        
REMARK   3    10  2.9722 -  2.8697    1.00     1186   132  0.2757 0.3614        
REMARK   3    11  2.8697 -  2.7799    0.99     1200   134  0.2978 0.3383        
REMARK   3    12  2.7799 -  2.7005    1.00     1182   131  0.3217 0.3858        
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)     : 0.440            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 28.940           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
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      :  0.003           3572                                  
REMARK   3   ANGLE     :  0.756           4843                                  
REMARK   3   CHIRALITY :  0.028            539                                  
REMARK   3   PLANARITY :  0.005            611                                  
REMARK   3   DIHEDRAL  : 12.795           1311                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 55 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -26.6252  28.7509  -1.4799              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4380 T22:   0.4231                                     
REMARK   3      T33:   0.2513 T12:   0.0797                                     
REMARK   3      T13:  -0.0038 T23:  -0.1028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2847 L22:   0.1115                                     
REMARK   3      L33:   0.0083 L12:  -0.0958                                     
REMARK   3      L13:   0.0840 L23:  -0.0443                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4676 S12:  -0.1429 S13:   0.0766                       
REMARK   3      S21:   0.1524 S22:  -0.2447 S23:  -0.0441                       
REMARK   3      S31:   0.3073 S32:  -0.0014 S33:   0.0234                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 56 THROUGH 158 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -16.2010  36.8756  -9.8500              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3289 T22:   0.2434                                     
REMARK   3      T33:   0.3266 T12:   0.0214                                     
REMARK   3      T13:  -0.0633 T23:  -0.0366                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2880 L22:   0.3015                                     
REMARK   3      L33:   0.2357 L12:   0.0187                                     
REMARK   3      L13:  -0.1097 L23:  -0.1214                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1971 S12:  -0.0775 S13:  -0.0018                       
REMARK   3      S21:   0.0055 S22:   0.2108 S23:  -0.0304                       
REMARK   3      S31:  -0.1316 S32:  -0.0521 S33:  -0.0037                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 159 THROUGH 296 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.2945  32.8794 -25.7901              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2876 T22:   0.3426                                     
REMARK   3      T33:   0.3696 T12:  -0.0743                                     
REMARK   3      T13:   0.0305 T23:  -0.0872                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3518 L22:   0.2486                                     
REMARK   3      L33:   0.4187 L12:  -0.0742                                     
REMARK   3      L13:   0.0998 L23:   0.2310                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1106 S12:   0.2435 S13:   0.0342                       
REMARK   3      S21:  -0.2098 S22:   0.1613 S23:  -0.2434                       
REMARK   3      S31:  -0.0320 S32:   0.1269 S33:   0.0001                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 69 THROUGH 79 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   4.3486  21.4377  19.9810              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9930 T22:   1.1710                                     
REMARK   3      T33:   0.3957 T12:  -0.4548                                     
REMARK   3      T13:  -0.5515 T23:   0.0099                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0141 L22:   0.0339                                     
REMARK   3      L33:   0.0408 L12:   0.0263                                     
REMARK   3      L13:   0.0266 L23:   0.0397                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0058 S12:  -0.1895 S13:  -0.0354                       
REMARK   3      S21:   0.0519 S22:   0.0038 S23:  -0.0091                       
REMARK   3      S31:  -0.0498 S32:   0.0384 S33:   0.0639                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 80 THROUGH 97 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   4.0637  10.6217   8.2553              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6574 T22:   0.0960                                     
REMARK   3      T33:   1.1690 T12:   0.0042                                     
REMARK   3      T13:  -0.3464 T23:   0.1828                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0027 L22:   0.0127                                     
REMARK   3      L33:  -0.0012 L12:   0.0030                                     
REMARK   3      L13:   0.0025 L23:   0.0063                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2371 S12:   0.0281 S13:  -0.2994                       
REMARK   3      S21:   0.2061 S22:  -0.0477 S23:  -0.2635                       
REMARK   3      S31:   0.1163 S32:  -0.0308 S33:   0.0513                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 98 THROUGH 119 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.8778  24.4370  15.1181              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4199 T22:   0.5417                                     
REMARK   3      T33:   0.3110 T12:  -0.1263                                     
REMARK   3      T13:  -0.1260 T23:   0.0996                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2365 L22:   0.4790                                     
REMARK   3      L33:   0.4802 L12:  -0.0621                                     
REMARK   3      L13:  -0.3141 L23:   0.2234                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6587 S12:  -0.5094 S13:  -0.4953                       
REMARK   3      S21:   0.4246 S22:  -0.3034 S23:  -0.3444                       
REMARK   3      S31:   0.0410 S32:   0.0311 S33:   0.3383                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 120 THROUGH 134 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.9478  17.7265   9.1717              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2768 T22:   0.3963                                     
REMARK   3      T33:   0.2923 T12:  -0.1493                                     
REMARK   3      T13:  -0.0756 T23:   0.0185                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3450 L22:   0.3281                                     
REMARK   3      L33:   0.0955 L12:  -0.3123                                     
REMARK   3      L13:  -0.0689 L23:   0.0033                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1493 S12:   0.1927 S13:  -0.1408                       
REMARK   3      S21:   0.1696 S22:  -0.3439 S23:   0.0163                       
REMARK   3      S31:   0.0672 S32:  -0.1184 S33:  -0.0321                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 135 THROUGH 156 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -8.1055   8.1972   4.7681              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5072 T22:   0.4256                                     
REMARK   3      T33:   0.6087 T12:  -0.1575                                     
REMARK   3      T13:  -0.0826 T23:  -0.0178                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1189 L22:   0.0757                                     
REMARK   3      L33:   0.1238 L12:  -0.0840                                     
REMARK   3      L13:  -0.0847 L23:   0.0653                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1333 S12:   0.3259 S13:  -0.4429                       
REMARK   3      S21:   0.1880 S22:  -0.1899 S23:  -0.5707                       
REMARK   3      S31:   0.1475 S32:  -0.1494 S33:   0.0091                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 157 THROUGH 170 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -15.2409  18.4774  10.5116              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4074 T22:   0.5765                                     
REMARK   3      T33:   0.2074 T12:  -0.0505                                     
REMARK   3      T13:  -0.0214 T23:  -0.0369                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0051 L22:   0.0107                                     
REMARK   3      L33:   0.0207 L12:   0.0096                                     
REMARK   3      L13:  -0.0301 L23:  -0.0036                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0870 S12:  -0.3553 S13:  -0.2679                       
REMARK   3      S21:   0.1106 S22:   0.0239 S23:   0.0291                       
REMARK   3      S31:  -0.1231 S32:  -0.4106 S33:   0.0005                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 171 THROUGH 185 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.0377  31.3792   7.4226              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2808 T22:   0.2695                                     
REMARK   3      T33:   0.3647 T12:  -0.1094                                     
REMARK   3      T13:  -0.0391 T23:  -0.0598                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4005 L22:   0.0124                                     
REMARK   3      L33:   0.2953 L12:  -0.0111                                     
REMARK   3      L13:  -0.0451 L23:  -0.0056                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0796 S12:  -0.0248 S13:   0.3926                       
REMARK   3      S21:   0.0659 S22:  -0.0309 S23:  -0.2580                       
REMARK   3      S31:  -0.2897 S32:  -0.2717 S33:   0.0081                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 186 THROUGH 192 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  11.8555  25.5182  14.1327              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2963 T22:   0.3562                                     
REMARK   3      T33:   1.0119 T12:  -0.4125                                     
REMARK   3      T13:  -0.5231 T23:   0.1896                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0301 L22:  -0.0017                                     
REMARK   3      L33:  -0.0027 L12:  -0.0012                                     
REMARK   3      L13:   0.0033 L23:  -0.0032                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0409 S12:  -0.0063 S13:  -0.0518                       
REMARK   3      S21:   0.0747 S22:   0.0264 S23:  -0.0507                       
REMARK   3      S31:   0.0492 S32:   0.0049 S33:   0.0352                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 193 THROUGH 201 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  10.2044  18.6373   5.6549              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2004 T22:   0.6323                                     
REMARK   3      T33:   0.9561 T12:   0.1012                                     
REMARK   3      T13:  -0.3438 T23:   0.2644                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0270 L22:   0.0773                                     
REMARK   3      L33:   0.0005 L12:  -0.0541                                     
REMARK   3      L13:   0.0122 L23:  -0.0132                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1102 S12:  -0.3371 S13:  -0.2904                       
REMARK   3      S21:  -0.0472 S22:  -0.0271 S23:  -0.0950                       
REMARK   3      S31:   0.1086 S32:   0.1219 S33:  -0.1295                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5UQ2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000226046.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-JUL-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 273                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 S 6M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16255                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 85.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 8.000                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 1.28000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1M LITHIUM CHLORIDE, 12% PEG 6000, AND   
REMARK 280  0.1M MES PH 6.2, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
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   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       38.55500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       60.45500            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       60.45500            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       19.27750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       60.45500            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       60.45500            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       57.83250            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       60.45500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       60.45500            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       19.27750            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       60.45500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       60.45500            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       57.83250            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       38.55500            
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: 2560 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -6.0 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 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 A    -2                                                      
REMARK 465     GLU A    -1                                                      
REMARK 465     PHE A     0                                                      
REMARK 465     ARG A   297                                                      
REMARK 465     LEU A   298                                                      
REMARK 465     GLY B    54                                                      
REMARK 465     ALA B    55                                                      
REMARK 465     MET B    56                                                      
REMARK 465     ASP B    57                                                      
REMARK 465     PRO B    58                                                      
REMARK 465     GLU B    59                                                      
REMARK 465     PHE B    60                                                      
REMARK 465     GLY B    61                                                      
REMARK 465     PRO B    62                                                      
REMARK 465     CYS B    63                                                      
REMARK 465     LEU B    64                                                      
REMARK 465     VAL B    65                                                      
REMARK 465     ILE B    66                                                      
REMARK 465     GLN B    67                                                      
REMARK 465     ARG B    68                                                      
REMARK 465     HIS B   202                                                      
REMARK 465     HIS B   203                                                      
REMARK 465     SER B   204                                                      
REMARK 465     GLY B   205                                                      
REMARK 465     ALA B   206                                                      
REMARK 465     VAL B   207                                                      
REMARK 465     ARG B   208                                                      
REMARK 465     ASN B   209                                                      
REMARK 465     TYR B   210                                                      
REMARK 465     ASN B   211                                                      
REMARK 465     ARG B   212                                                      
REMARK 465     ASP B   213                                                      
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     LYS A  24    CG   CD   CE   NZ                                   
REMARK 470     GLU A  28    CG   CD   OE1  OE2                                  
REMARK 470     TYR A 179    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN A 246    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 250    CG   CD   CE   NZ                                   
REMARK 470     ASP B  79    CG   OD1  OD2                                       
REMARK 470     ASP B  81    CG   OD1  OD2                                       
REMARK 470     GLN B  84    CG   CD   OE1  NE2                                  
REMARK 470     TRP B  88    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP B  88    CZ3  CH2                                            
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   O    ASP A   145     O    HOH A   301              1.94            
REMARK 500   OH   TYR B   128     O    HOH B   301              2.08            
REMARK 500   OE2  GLU B   184     O    HOH B   302              2.08            
REMARK 500   OE1  GLU B   137     OG1  THR B   140              2.15            
REMARK 500   OH   TYR A   107     O    HOH A   302              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   CB   CYS B    91     SG   CYS B    92     7555     1.36            
REMARK 500   O    THR A    39     NH1  ARG A   217     8554     2.18            
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    GLU A   2     -144.68     54.83                                   
REMARK 500    LYS A  24     -164.62    -75.04                                   
REMARK 500    LEU A  25      -32.19     61.83                                   
REMARK 500    THR A  26      -43.99   -132.95                                   
REMARK 500    ASP A 127       44.40   -143.25                                   
REMARK 500    ASP A 145       78.50     56.22                                   
REMARK 500    PHE A 146       31.43    -94.75                                   
REMARK 500    VAL A 156       53.00     29.21                                   
REMARK 500    GLU A 162       84.30    -67.26                                   
REMARK 500    TYR A 179        6.38    150.63                                   
REMARK 500    SER A 181     -143.54   -146.47                                   
REMARK 500    ASP A 223     -166.71   -116.12                                   
REMARK 500    PRO A 284       25.96    -67.27                                   
REMARK 500    GLU B 137       93.21    -69.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5UQ1   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 5UQ3   RELATED DB: PDB                                   
DBREF  5UQ2 A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  5UQ2 B   61   213  UNP    Q5MJ70   SPDYA_HUMAN     61    213             
SEQADV 5UQ2 GLY A   -2  UNP  P24941              EXPRESSION TAG                 
SEQADV 5UQ2 GLU A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 5UQ2 PHE A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 5UQ2 GLY B   54  UNP  Q5MJ70              EXPRESSION TAG                 
SEQADV 5UQ2 ALA B   55  UNP  Q5MJ70              EXPRESSION TAG                 
SEQADV 5UQ2 MET B   56  UNP  Q5MJ70              EXPRESSION TAG                 
SEQADV 5UQ2 ASP B   57  UNP  Q5MJ70              EXPRESSION TAG                 
SEQADV 5UQ2 PRO B   58  UNP  Q5MJ70              EXPRESSION TAG                 
SEQADV 5UQ2 GLU B   59  UNP  Q5MJ70              EXPRESSION TAG                 
SEQADV 5UQ2 PHE B   60  UNP  Q5MJ70              EXPRESSION TAG                 
SEQRES   1 A  301  GLY GLU PHE MET GLU ASN PHE GLN LYS VAL GLU LYS ILE          
SEQRES   2 A  301  GLY GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN          
SEQRES   3 A  301  LYS LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG          
SEQRES   4 A  301  LEU ASP THR GLU THR GLU GLY VAL PRO SER THR ALA ILE          
SEQRES   5 A  301  ARG GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN          
SEQRES   6 A  301  ILE VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS          
SEQRES   7 A  301  LEU TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS          
SEQRES   8 A  301  LYS PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU          
SEQRES   9 A  301  PRO LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY          
SEQRES  10 A  301  LEU ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP          
SEQRES  11 A  301  LEU LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA          
SEQRES  12 A  301  ILE LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY          
SEQRES  13 A  301  VAL PRO VAL ARG THR TYR THR HIS GLU VAL VAL THR LEU          
SEQRES  14 A  301  TRP TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR          
SEQRES  15 A  301  TYR SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE          
SEQRES  16 A  301  PHE ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY          
SEQRES  17 A  301  ASP SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR          
SEQRES  18 A  301  LEU GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR          
SEQRES  19 A  301  SER MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA          
SEQRES  20 A  301  ARG GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU          
SEQRES  21 A  301  ASP GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP          
SEQRES  22 A  301  PRO ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS          
SEQRES  23 A  301  PRO PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU          
SEQRES  24 A  301  ARG LEU                                                      
SEQRES   1 B  160  GLY ALA MET ASP PRO GLU PHE GLY PRO CYS LEU VAL ILE          
SEQRES   2 B  160  GLN ARG GLN ASP MET THR ALA PHE PHE LYS LEU PHE ASP          
SEQRES   3 B  160  ASP ASP LEU ILE GLN ASP PHE LEU TRP MET ASP CYS CYS          
SEQRES   4 B  160  CYS LYS ILE ALA ASP LYS TYR LEU LEU ALA MET THR PHE          
SEQRES   5 B  160  VAL TYR PHE LYS ARG ALA LYS PHE THR ILE SER GLU HIS          
SEQRES   6 B  160  THR ARG ILE ASN PHE PHE ILE ALA LEU TYR LEU ALA ASN          
SEQRES   7 B  160  THR VAL GLU GLU ASP GLU GLU GLU THR LYS TYR GLU ILE          
SEQRES   8 B  160  PHE PRO TRP ALA LEU GLY LYS ASN TRP ARG LYS LEU PHE          
SEQRES   9 B  160  PRO ASN PHE LEU LYS LEU ARG ASP GLN LEU TRP ASP ARG          
SEQRES  10 B  160  ILE ASP TYR ARG ALA ILE VAL SER ARG ARG CYS CYS GLU          
SEQRES  11 B  160  GLU VAL MET ALA ILE ALA PRO THR HIS TYR ILE TRP GLN          
SEQRES  12 B  160  ARG GLU ARG SER VAL HIS HIS SER GLY ALA VAL ARG ASN          
SEQRES  13 B  160  TYR ASN ARG ASP                                              
FORMUL   3  HOH   *23(H2 O)                                                     
HELIX    1 AA1 PRO A   45  LYS A   56  1                                  12    
HELIX    2 AA2 LEU A   87  SER A   94  1                                   8    
HELIX    3 AA3 PRO A  100  HIS A  121  1                                  22    
HELIX    4 AA4 LYS A  129  GLN A  131  5                                   3    
HELIX    5 AA5 THR A  165  ARG A  169  5                                   5    
HELIX    6 AA6 ALA A  170  LEU A  175  1                                   6    
HELIX    7 AA7 THR A  182  THR A  198  1                                  17    
HELIX    8 AA8 SER A  207  GLY A  220  1                                  14    
HELIX    9 AA9 ASP A  247  VAL A  252  1                                   6    
HELIX   10 AB1 ASP A  256  LEU A  267  1                                  12    
HELIX   11 AB2 SER A  276  ALA A  282  1                                   7    
HELIX   12 AB3 MET B   71  LYS B   76  1                                   6    
HELIX   13 AB4 LEU B   77  ASP B   79  5                                   3    
HELIX   14 AB5 ASP B   80  ASP B   90  1                                  11    
HELIX   15 AB6 ASP B   97  ALA B  111  1                                  15    
HELIX   16 AB7 THR B  114  HIS B  118  5                                   5    
HELIX   17 AB8 THR B  119  GLU B  135  1                                  17    
HELIX   18 AB9 GLU B  139  TYR B  142  5                                   4    
HELIX   19 AC1 GLU B  143  GLY B  150  1                                   8    
HELIX   20 AC2 ASN B  152  LYS B  155  5                                   4    
HELIX   21 AC3 LEU B  156  ILE B  171  1                                  16    
HELIX   22 AC4 SER B  178  MET B  186  1                                   9    
HELIX   23 AC5 HIS B  192  ARG B  197  5                                   6    
SHEET    1 AA1 5 PHE A   4  GLU A  12  0                                        
SHEET    2 AA1 5 GLY A  16  ASN A  23 -1  O  LYS A  20   N  GLU A   8           
SHEET    3 AA1 5 VAL A  29  ILE A  35 -1  O  LEU A  32   N  TYR A  19           
SHEET    4 AA1 5 LEU A  76  GLU A  81 -1  O  LEU A  78   N  LYS A  33           
SHEET    5 AA1 5 LEU A  66  HIS A  71 -1  N  ASP A  68   O  VAL A  79           
SHEET    1 AA2 3 GLN A  85  ASP A  86  0                                        
SHEET    2 AA2 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3 AA2 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1 AA3 2 VAL A 123  LEU A 124  0                                        
SHEET    2 AA3 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SSBOND   1 CYS B   91    CYS B   92                          1555   7555  2.03  
CRYST1  120.910  120.910   77.110  90.00  90.00  90.00 P 41 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      0.008271  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008271  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012969        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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