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Database: PDB
Entry: 3BLQ
LinkDB: 3BLQ
Original site: 3BLQ 
HEADER    TRANSCRIPTION                           11-DEC-07   3BLQ              
TITLE     CRYSTAL STRUCTURE OF HUMAN CDK9/CYCLINT1 IN COMPLEX WITH ATP          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION PROTEIN KINASE 9;                            
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 2-330;                                        
COMPND   5 SYNONYM: CYCLIN-DEPENDENT KINASE 9, SERINE/THREONINE-PROTEIN KINASE  
COMPND   6 PITALRE, C-2K, CELL DIVISION CYCLE 2-LIKE PROTEIN KINASE 4;          
COMPND   7 EC: 2.7.11.22, 2.7.11.23;                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: CYCLIN-T1;                                                 
COMPND  11 CHAIN: B;                                                            
COMPND  12 FRAGMENT: UNP RESIDUES 2-259;                                        
COMPND  13 SYNONYM: CYCT1, CYCLIN-T;                                            
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDK9;                                                          
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULO VIRUS;                         
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PVL1392;                                  
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 GENE: CCNT1;                                                         
SOURCE  17 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE  18 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE  19 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE  20 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE  21 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULO VIRUS;                         
SOURCE  22 EXPRESSION_SYSTEM_PLASMID: PVL1392                                   
KEYWDS    TRANSCRIPTIONAL CDK-CYCLIN COMPLEX, PHOSPHORYLATED, IN COMPLEX WITH   
KEYWDS   2 ATP, ALTERNATIVE SPLICING, ATP-BINDING, KINASE, NUCLEOTIDE-BINDING,  
KEYWDS   3 NUCLEUS, PHOSPHOPROTEIN, POLYMORPHISM, SERINE/THREONINE-PROTEIN      
KEYWDS   4 KINASE, TRANSCRIPTION REGULATION, TRANSFERASE, ACETYLATION, CELL     
KEYWDS   5 CYCLE, CELL DIVISION, COILED COIL, HOST-VIRUS INTERACTION,           
KEYWDS   6 TRANSCRIPTION                                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.BAUMLI,G.LOLLI,E.D.LOWE,L.N.JOHNSON                                 
REVDAT   5   25-OCT-17 3BLQ    1       REMARK                                   
REVDAT   4   19-MAY-09 3BLQ    1       REMARK                                   
REVDAT   3   24-FEB-09 3BLQ    1       VERSN                                    
REVDAT   2   12-AUG-08 3BLQ    1       JRNL                                     
REVDAT   1   01-JUL-08 3BLQ    0                                                
JRNL        AUTH   S.BAUMLI,G.LOLLI,E.D.LOWE,S.TROIANI,L.RUSCONI,A.N.BULLOCK,   
JRNL        AUTH 2 J.E.DEBRECZENI,S.KNAPP,L.N.JOHNSON                           
JRNL        TITL   THE STRUCTURE OF P-TEFB (CDK9/CYCLIN T1), ITS COMPLEX WITH   
JRNL        TITL 2 FLAVOPIRIDOL AND REGULATION BY PHOSPHORYLATION               
JRNL        REF    EMBO J.                       V.  27  1907 2008              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   18566585                                                     
JRNL        DOI    10.1038/EMBOJ.2008.121                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.50                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 23638                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.234                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2366                            
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 29.5020 - 12.6070    0.82      439     0  0.2290 0.0000        
REMARK   3     2 12.6070 - 10.1390    0.93      493     0  0.1340 0.0000        
REMARK   3     3 10.1390 -  8.8980    0.93      499     0  0.1230 0.0000        
REMARK   3     4  8.8980 -  8.1030    0.95      490     0  0.1280 0.0000        
REMARK   3     5  8.1030 -  7.5320    0.93      490     0  0.1480 0.0000        
REMARK   3     6  7.5320 -  7.0950    0.95      531     0  0.1580 0.0000        
REMARK   3     7  7.0950 -  6.7440    0.95      510     0  0.1700 0.0000        
REMARK   3     8  6.7440 -  6.4540    0.91      473     0  0.1800 0.0000        
REMARK   3     9  6.4540 -  6.2080    0.95      486     0  0.1770 0.0000        
REMARK   3    10  6.2080 -  5.9950    0.95      508     0  0.1750 0.0000        
REMARK   3    11  5.9950 -  5.8090    0.94      499     0  0.1600 0.0000        
REMARK   3    12  5.8090 -  5.6440    0.94      500     0  0.1630 0.0000        
REMARK   3    13  5.6440 -  5.4970    0.96      536     0  0.1700 0.0000        
REMARK   3    14  5.4970 -  5.3640    0.95      500     0  0.1400 0.0000        
REMARK   3    15  5.3640 -  5.2420    0.95      462     0  0.1700 0.0000        
REMARK   3    16  5.2420 -  5.1310    0.96      564     0  0.1410 0.0000        
REMARK   3    17  5.1310 -  5.0290    0.92      475     0  0.1400 0.0000        
REMARK   3    18  5.0290 -  4.9350    0.95      481     0  0.1280 0.0000        
REMARK   3    19  4.9350 -  4.8470    0.94      549     0  0.1360 0.0000        
REMARK   3    20  4.8470 -  4.7650    0.95      444     0  0.1190 0.0000        
REMARK   3    21  4.7650 -  4.6890    0.93      529     0  0.1390 0.0000        
REMARK   3    22  4.6890 -  4.6170    0.93      505     0  0.1230 0.0000        
REMARK   3    23  4.6170 -  4.5490    0.95      474     0  0.1370 0.0000        
REMARK   3    24  4.5490 -  4.4850    0.95      539     0  0.1240 0.0000        
REMARK   3    25  4.4850 -  4.4250    0.96      518     0  0.1290 0.0000        
REMARK   3    26  4.4250 -  4.3670    0.94      455     0  0.1430 0.0000        
REMARK   3    27  4.3670 -  4.3130    0.96      555     0  0.1270 0.0000        
REMARK   3    28  4.3130 -  4.2610    0.93      497     0  0.1340 0.0000        
REMARK   3    29  4.2610 -  4.2120    0.96      489     0  0.1420 0.0000        
REMARK   3    30  4.2120 -  4.1650    0.95      495     0  0.1250 0.0000        
REMARK   3    31  4.1650 -  4.1200    0.96      531     0  0.1300 0.0000        
REMARK   3    32  4.1200 -  4.0760    0.93      497     0  0.1600 0.0000        
REMARK   3    33  4.0760 -  4.0350    0.95      442     0  0.1320 0.0000        
REMARK   3    34  4.0350 -  3.9950    0.94      563     0  0.1290 0.0000        
REMARK   3    35  3.9950 -  3.9570    0.93      483     0  0.1550 0.0000        
REMARK   3    36  3.9570 -  3.9200    0.96      523     0  0.1490 0.0000        
REMARK   3    37  3.9200 -  3.8840    0.95      462     0  0.1530 0.0000        
REMARK   3    38  3.8840 -  3.8500    0.92      503     0  0.1560 0.0000        
REMARK   3    39  3.8500 -  3.8170    0.95      513     0  0.1530 0.0000        
REMARK   3    40  3.8170 -  3.7850    0.95      521     0  0.1590 0.0000        
REMARK   3    41  3.7850 -  3.7540    0.95      461     0  0.1580 0.0000        
REMARK   3    42  3.7540 -  3.7240    0.97      556     0  0.1670 0.0000        
REMARK   3    43  3.7240 -  3.6950    0.92      498     0  0.1530 0.0000        
REMARK   3    44  3.6950 -  3.6670    0.93      507     0  0.1790 0.0000        
REMARK   3    45  3.6670 -  3.6390    0.95      486     0  0.1480 0.0000        
REMARK   3    46  3.6390 -  3.6130    0.95      476     0  0.1580 0.0000        
REMARK   3    47  3.6130 -  3.5870    0.96      520     0  0.1630 0.0000        
REMARK   3    48  3.5870 -  3.5620    0.95      584     0  0.1710 0.0000        
REMARK   3    49  3.5620 -  3.5380    0.91      428     0  0.1760 0.0000        
REMARK   3    50  3.5380 -  3.5140    0.91      493     0  0.1800 0.0000        
REMARK   3    51  3.5140 -  3.4910    0.91      441     0  0.1730 0.0000        
REMARK   3    52  3.4910 -  3.4680    0.94      546     0  0.1770 0.0000        
REMARK   3    53  3.4680 -  3.4460    0.97      512     0  0.1860 0.0000        
REMARK   3    54  3.4460 -  3.4250    0.94      532     0  0.1800 0.0000        
REMARK   3    55  3.4250 -  3.4040    0.96      483     0  0.1790 0.0000        
REMARK   3    56  3.4040 -  3.3840    0.94      478     0  0.1950 0.0000        
REMARK   3    57  3.3840 -  3.3640    0.93      504     0  0.2080 0.0000        
REMARK   3    58  3.3640 -  3.3450    0.94      530     0  0.1970 0.0000        
REMARK   3    59  3.3450 -  3.3260    0.95      501     0  0.1930 0.0000        
REMARK   3    60  3.3260 -  3.3070    0.96      468     0  0.2180 0.0000        
REMARK   3    61  3.3070 -  3.2890    0.94      475     0  0.2190 0.0000        
REMARK   3    62  3.2890 -  3.2710    0.95      547     0  0.1960 0.0000        
REMARK   3    63  3.2710 -  3.2540    0.96      526     0  0.1940 0.0000        
REMARK   3    64  3.2540 -  3.2370    0.95      502     0  0.2160 0.0000        
REMARK   3    65  3.2370 -  3.2200    0.95      502     0  0.2070 0.0000        
REMARK   3    66  3.2200 -  3.2040    0.95      475     0  0.1990 0.0000        
REMARK   3    67  3.2040 -  3.1880    0.94      503     0  0.2270 0.0000        
REMARK   3    68  3.1880 -  3.1720    0.93      509     0  0.2240 0.0000        
REMARK   3    69  3.1720 -  3.1570    0.95      494     0  0.2060 0.0000        
REMARK   3    70  3.1570 -  3.1420    0.94      529     0  0.1920 0.0000        
REMARK   3    71  3.1420 -  3.1270    0.93      511     0  0.2380 0.0000        
REMARK   3    72  3.1270 -  3.1120    0.94      495     0  0.2180 0.0000        
REMARK   3    73  3.1120 -  3.0980    0.96      480     0  0.2350 0.0000        
REMARK   3    74  3.0980 -  3.0840    0.95      490     0  0.2100 0.0000        
REMARK   3    75  3.0840 -  3.0700    0.92      532     0  0.2200 0.0000        
REMARK   3    76  3.0700 -  3.0570    0.94      470     0  0.2530 0.0000        
REMARK   3    77  3.0570 -  3.0430    0.94      522     0  0.2330 0.0000        
REMARK   3    78  3.0430 -  3.0300    0.95      488     0  0.2480 0.0000        
REMARK   3    79  3.0300 -  3.0180    0.93      545     0  0.2300 0.0000        
REMARK   3    80  3.0180 -  3.0050    0.97      490     0  0.2350 0.0000        
REMARK   3    81  3.0050 -  2.9930    0.94      447     0  0.2630 0.0000        
REMARK   3    82  2.9930 -  2.9800    0.94      531     0  0.2460 0.0000        
REMARK   3    83  2.9800 -  2.9680    0.94      495     0  0.2790 0.0000        
REMARK   3    84  2.9680 -  2.9570    0.94      513     0  0.2490 0.0000        
REMARK   3    85  2.9570 -  2.9450    0.92      487     0  0.2580 0.0000        
REMARK   3    86  2.9450 -  2.9340    0.93      511     0  0.2620 0.0000        
REMARK   3    87  2.9340 -  2.9220    0.96      511     0  0.2680 0.0000        
REMARK   3    88  2.9220 -  2.9110    0.95      470     0  0.2660 0.0000        
REMARK   3    89  2.9110 -  2.9000    0.95      517     0  0.2520 0.0000        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3   K_SOL              : 0.31                                          
REMARK   3   B_SOL              : 47.84                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : NULL             
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 84.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.05600                                             
REMARK   3    B22 (A**2) : -1.05600                                             
REMARK   3    B33 (A**2) : 2.11300                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  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      :  0.006           NULL                                  
REMARK   3   ANGLE     :  0.745           NULL                                  
REMARK   3   CHIRALITY :  0.055           NULL                                  
REMARK   3   PLANARITY :  0.003           NULL                                  
REMARK   3   DIHEDRAL  : 11.205           NULL                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  46.8817 -17.5246  -1.5063              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3306 T22:   0.2130                                     
REMARK   3      T33:   0.4583 T12:  -0.0056                                     
REMARK   3      T13:  -0.0935 T23:   0.0706                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4354 L22:   1.2988                                     
REMARK   3      L33:   2.6247 L12:  -0.0773                                     
REMARK   3      L13:   0.2117 L23:   0.4837                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2677 S12:   0.0668 S13:  -0.6278                       
REMARK   3      S21:   0.2104 S22:  -0.1728 S23:  -0.1872                       
REMARK   3      S31:   0.7499 S32:   0.1817 S33:  -0.0962                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  21.4156   3.4648 -20.4795              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2072 T22:   0.3008                                     
REMARK   3      T33:   0.2741 T12:  -0.0113                                     
REMARK   3      T13:  -0.0270 T23:  -0.0513                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1487 L22:   1.1302                                     
REMARK   3      L33:   1.2323 L12:  -0.4348                                     
REMARK   3      L13:  -0.1180 L23:   0.2001                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0383 S12:   0.2440 S13:   0.2651                       
REMARK   3      S21:   0.0105 S22:   0.0855 S23:  -0.2873                       
REMARK   3      S31:  -0.0902 S32:   0.1227 S33:  -0.1151                       
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 3BLQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 13-DEC-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000045674.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-NOV-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.93300                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM, DENZO                      
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23641                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 5.200                              
REMARK 200  R MERGE                    (I) : 0.08500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.51200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3BLH                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.60                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, 20% PEG 1000, 0.5M NACL,      
REMARK 280  4MM TCEP, 2MM AMPPNP, 2.4MM MGCL2, PH 8.5, VAPOR DIFFUSION,         
REMARK 280  SITTING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: H 3                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   X+2/3,Y+1/3,Z+1/3                                       
REMARK 290       5555   -Y+2/3,X-Y+1/3,Z+1/3                                    
REMARK 290       6555   -X+Y+2/3,-X+1/3,Z+1/3                                   
REMARK 290       7555   X+1/3,Y+2/3,Z+2/3                                       
REMARK 290       8555   -Y+1/3,X-Y+2/3,Z+2/3                                    
REMARK 290       9555   -X+Y+1/3,-X+2/3,Z+2/3                                   
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       86.56500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       49.97833            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       31.88000            
REMARK 290   SMTRY1   5 -0.500000 -0.866025  0.000000       86.56500            
REMARK 290   SMTRY2   5  0.866025 -0.500000  0.000000       49.97833            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       31.88000            
REMARK 290   SMTRY1   6 -0.500000  0.866025  0.000000       86.56500            
REMARK 290   SMTRY2   6 -0.866025 -0.500000  0.000000       49.97833            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       31.88000            
REMARK 290   SMTRY1   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       99.95665            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       63.76000            
REMARK 290   SMTRY1   8 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.866025 -0.500000  0.000000       99.95665            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       63.76000            
REMARK 290   SMTRY1   9 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025 -0.500000  0.000000       99.95665            
REMARK 290   SMTRY3   9  0.000000  0.000000  1.000000       63.76000            
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: 2820 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 27240 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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     0                                                      
REMARK 465     PRO A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     TYR A     5                                                      
REMARK 465     ASP A     6                                                      
REMARK 465     LYS A    88                                                      
REMARK 465     ALA A    89                                                      
REMARK 465     SER A    90                                                      
REMARK 465     PRO A    91                                                      
REMARK 465     TYR A    92                                                      
REMARK 465     ASN A    93                                                      
REMARK 465     ARG A    94                                                      
REMARK 465     CYS A    95                                                      
REMARK 465     LYS A    96                                                      
REMARK 465     GLY A    97                                                      
REMARK 465     LEU A   176                                                      
REMARK 465     ALA A   177                                                      
REMARK 465     LYS A   178                                                      
REMARK 465     ASN A   179                                                      
REMARK 465     SER A   180                                                      
REMARK 465     GLN A   181                                                      
REMARK 465     PRO A   182                                                      
REMARK 465     LYS A   269                                                      
REMARK 465     GLY A   270                                                      
REMARK 465     GLN A   271                                                      
REMARK 465     LYS A   272                                                      
REMARK 465     ARG A   273                                                      
REMARK 465     LYS A   274                                                      
REMARK 465     GLY A   326                                                      
REMARK 465     MET A   327                                                      
REMARK 465     LEU A   328                                                      
REMARK 465     SER A   329                                                      
REMARK 465     THR A   330                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     PRO B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     GLY B     3                                                      
REMARK 465     GLU B     4                                                      
REMARK 465     ARG B     5                                                      
REMARK 465     LYS B     6                                                      
REMARK 465     ASN B     7                                                      
REMARK 465     ASN B     8                                                      
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    CYS A  10       51.35   -145.63                                   
REMARK 500    PRO A  11      -37.75    -38.94                                   
REMARK 500    LYS A  18      -47.58    -27.85                                   
REMARK 500    ALA A  23      143.39    173.32                                   
REMARK 500    GLU A  53      -54.62   -133.23                                   
REMARK 500    VAL A  79      139.43    -34.64                                   
REMARK 500    ARG A  86     -163.22   -124.76                                   
REMARK 500    ASP A 167       82.78     61.72                                   
REMARK 500    VAL A 190      129.25     75.14                                   
REMARK 500    ARG A 204       14.77   -140.30                                   
REMARK 500    ASN A 232      -34.04   -134.89                                   
REMARK 500    GLN A 243       34.56    -82.00                                   
REMARK 500    LEU A 244      -42.30   -147.82                                   
REMARK 500    PRO A 250       -9.79    -56.96                                   
REMARK 500    PRO A 254      116.82    -37.02                                   
REMARK 500    ASN A 258      -31.74    -35.66                                   
REMARK 500    LEU A 261        5.87    -60.31                                   
REMARK 500    LEU A 265       82.83     82.93                                   
REMARK 500    ARG A 284      -59.23     75.65                                   
REMARK 500    LEU A 296       54.14    -93.28                                   
REMARK 500    ASP B  30      144.80    -38.41                                   
REMARK 500    ILE B  72      -44.17   -130.29                                   
REMARK 500    THR B 121        3.18    -62.02                                   
REMARK 500    LEU B 163       21.66    -75.79                                   
REMARK 500    VAL B 164       12.75   -140.52                                   
REMARK 500    ARG B 165       60.36     37.69                                   
REMARK 500    SER B 215      154.83    -45.72                                   
REMARK 500    VAL B 225      -32.15   -135.73                                   
REMARK 500    ASN B 250       -9.11     66.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 331                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 332                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS B 260                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3BLH   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HUMAN CDK9/CYCLINT1                                     
REMARK 900 RELATED ID: 3BLR   RELATED DB: PDB                                   
DBREF  3BLQ A    2   330  UNP    P50750   CDK9_HUMAN       2    330             
DBREF  3BLQ B    2   259  UNP    O60563   CCNT1_HUMAN      2    259             
SEQADV 3BLQ GLY A    0  UNP  P50750              EXPRESSION TAG                 
SEQADV 3BLQ PRO A    1  UNP  P50750              EXPRESSION TAG                 
SEQADV 3BLQ GLY B    0  UNP  O60563              EXPRESSION TAG                 
SEQADV 3BLQ PRO B    1  UNP  O60563              EXPRESSION TAG                 
SEQADV 3BLQ ARG B   77  UNP  O60563    GLN    77 ENGINEERED                     
SEQADV 3BLQ GLY B   96  UNP  O60563    GLU    96 ENGINEERED                     
SEQADV 3BLQ LEU B  241  UNP  O60563    PHE   241 ENGINEERED                     
SEQRES   1 A  331  GLY PRO ALA LYS GLN TYR ASP SER VAL GLU CYS PRO PHE          
SEQRES   2 A  331  CYS ASP GLU VAL SER LYS TYR GLU LYS LEU ALA LYS ILE          
SEQRES   3 A  331  GLY GLN GLY THR PHE GLY GLU VAL PHE LYS ALA ARG HIS          
SEQRES   4 A  331  ARG LYS THR GLY GLN LYS VAL ALA LEU LYS LYS VAL LEU          
SEQRES   5 A  331  MET GLU ASN GLU LYS GLU GLY PHE PRO ILE THR ALA LEU          
SEQRES   6 A  331  ARG GLU ILE LYS ILE LEU GLN LEU LEU LYS HIS GLU ASN          
SEQRES   7 A  331  VAL VAL ASN LEU ILE GLU ILE CYS ARG THR LYS ALA SER          
SEQRES   8 A  331  PRO TYR ASN ARG CYS LYS GLY SER ILE TYR LEU VAL PHE          
SEQRES   9 A  331  ASP PHE CYS GLU HIS ASP LEU ALA GLY LEU LEU SER ASN          
SEQRES  10 A  331  VAL LEU VAL LYS PHE THR LEU SER GLU ILE LYS ARG VAL          
SEQRES  11 A  331  MET GLN MET LEU LEU ASN GLY LEU TYR TYR ILE HIS ARG          
SEQRES  12 A  331  ASN LYS ILE LEU HIS ARG ASP MET LYS ALA ALA ASN VAL          
SEQRES  13 A  331  LEU ILE THR ARG ASP GLY VAL LEU LYS LEU ALA ASP PHE          
SEQRES  14 A  331  GLY LEU ALA ARG ALA PHE SER LEU ALA LYS ASN SER GLN          
SEQRES  15 A  331  PRO ASN ARG TYR TPO ASN ARG VAL VAL THR LEU TRP TYR          
SEQRES  16 A  331  ARG PRO PRO GLU LEU LEU LEU GLY GLU ARG ASP TYR GLY          
SEQRES  17 A  331  PRO PRO ILE ASP LEU TRP GLY ALA GLY CYS ILE MET ALA          
SEQRES  18 A  331  GLU MET TRP THR ARG SER PRO ILE MET GLN GLY ASN THR          
SEQRES  19 A  331  GLU GLN HIS GLN LEU ALA LEU ILE SER GLN LEU CYS GLY          
SEQRES  20 A  331  SER ILE THR PRO GLU VAL TRP PRO ASN VAL ASP ASN TYR          
SEQRES  21 A  331  GLU LEU TYR GLU LYS LEU GLU LEU VAL LYS GLY GLN LYS          
SEQRES  22 A  331  ARG LYS VAL LYS ASP ARG LEU LYS ALA TYR VAL ARG ASP          
SEQRES  23 A  331  PRO TYR ALA LEU ASP LEU ILE ASP LYS LEU LEU VAL LEU          
SEQRES  24 A  331  ASP PRO ALA GLN ARG ILE ASP SER ASP ASP ALA LEU ASN          
SEQRES  25 A  331  HIS ASP PHE PHE TRP SER ASP PRO MET PRO SER ASP LEU          
SEQRES  26 A  331  LYS GLY MET LEU SER THR                                      
SEQRES   1 B  260  GLY PRO GLU GLY GLU ARG LYS ASN ASN ASN LYS ARG TRP          
SEQRES   2 B  260  TYR PHE THR ARG GLU GLN LEU GLU ASN SER PRO SER ARG          
SEQRES   3 B  260  ARG PHE GLY VAL ASP PRO ASP LYS GLU LEU SER TYR ARG          
SEQRES   4 B  260  GLN GLN ALA ALA ASN LEU LEU GLN ASP MET GLY GLN ARG          
SEQRES   5 B  260  LEU ASN VAL SER GLN LEU THR ILE ASN THR ALA ILE VAL          
SEQRES   6 B  260  TYR MET HIS ARG PHE TYR MET ILE GLN SER PHE THR ARG          
SEQRES   7 B  260  PHE PRO GLY ASN SER VAL ALA PRO ALA ALA LEU PHE LEU          
SEQRES   8 B  260  ALA ALA LYS VAL GLU GLY GLN PRO LYS LYS LEU GLU HIS          
SEQRES   9 B  260  VAL ILE LYS VAL ALA HIS THR CYS LEU HIS PRO GLN GLU          
SEQRES  10 B  260  SER LEU PRO ASP THR ARG SER GLU ALA TYR LEU GLN GLN          
SEQRES  11 B  260  VAL GLN ASP LEU VAL ILE LEU GLU SER ILE ILE LEU GLN          
SEQRES  12 B  260  THR LEU GLY PHE GLU LEU THR ILE ASP HIS PRO HIS THR          
SEQRES  13 B  260  HIS VAL VAL LYS CYS THR GLN LEU VAL ARG ALA SER LYS          
SEQRES  14 B  260  ASP LEU ALA GLN THR SER TYR PHE MET ALA THR ASN SER          
SEQRES  15 B  260  LEU HIS LEU THR THR PHE SER LEU GLN TYR THR PRO PRO          
SEQRES  16 B  260  VAL VAL ALA CYS VAL CYS ILE HIS LEU ALA CYS LYS TRP          
SEQRES  17 B  260  SER ASN TRP GLU ILE PRO VAL SER THR ASP GLY LYS HIS          
SEQRES  18 B  260  TRP TRP GLU TYR VAL ASP ALA THR VAL THR LEU GLU LEU          
SEQRES  19 B  260  LEU ASP GLU LEU THR HIS GLU LEU LEU GLN ILE LEU GLU          
SEQRES  20 B  260  LYS THR PRO ASN ARG LEU LYS ARG ILE TRP ASN TRP ARG          
MODRES 3BLQ TPO A  186  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 186      11                                                       
HET     MG  A 331       1                                                       
HET    ATP  A 332      31                                                       
HET    TRS  B 260       8                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     TPO PHOSPHONOTHREONINE                                               
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   3   MG    MG 2+                                                        
FORMUL   4  ATP    C10 H16 N5 O13 P3                                            
FORMUL   5  TRS    C4 H12 N O3 1+                                               
FORMUL   6  HOH   *30(H2 O)                                                     
HELIX    1   1 GLU A   15  SER A   17  5                                   3    
HELIX    2   2 PRO A   60  LEU A   73  1                                  14    
HELIX    3   3 LEU A  110  ASN A  116  1                                   7    
HELIX    4   4 THR A  122  ASN A  143  1                                  22    
HELIX    5   5 LYS A  151  ALA A  153  5                                   3    
HELIX    6   6 THR A  191  ARG A  195  5                                   5    
HELIX    7   7 PRO A  196  LEU A  201  1                                   6    
HELIX    8   8 PRO A  208  ARG A  225  1                                  18    
HELIX    9   9 THR A  233  GLY A  246  1                                  14    
HELIX   10  10 TYR A  259  LYS A  264  5                                   6    
HELIX   11  11 LEU A  279  ARG A  284  1                                   6    
HELIX   12  12 ASP A  285  LEU A  296  1                                  12    
HELIX   13  13 ASP A  305  HIS A  312  1                                   8    
HELIX   14  14 ASP A  313  TRP A  316  5                                   4    
HELIX   15  15 THR B   15  ASN B   21  1                                   7    
HELIX   16  16 SER B   22  PHE B   27  1                                   6    
HELIX   17  17 ASP B   30  ASN B   53  1                                  24    
HELIX   18  18 SER B   55  TYR B   70  1                                  16    
HELIX   19  19 PRO B   79  GLU B   95  1                                  17    
HELIX   20  20 LYS B  100  HIS B  113  1                                  14    
HELIX   21  21 SER B  123  LEU B  144  1                                  22    
HELIX   22  22 HIS B  152  THR B  161  1                                  10    
HELIX   23  23 SER B  167  THR B  185  1                                  19    
HELIX   24  24 THR B  186  GLN B  190  5                                   5    
HELIX   25  25 THR B  192  SER B  208  1                                  17    
HELIX   26  26 HIS B  220  VAL B  225  5                                   6    
HELIX   27  27 THR B  230  THR B  248  1                                  19    
HELIX   28  28 ASN B  250  TRP B  256  1                                   7    
SHEET    1   A 5 TYR A  19  GLN A  27  0                                        
SHEET    2   A 5 GLU A  32  HIS A  38 -1  O  VAL A  33   N  ILE A  25           
SHEET    3   A 5 LYS A  44  VAL A  50 -1  O  LEU A  47   N  PHE A  34           
SHEET    4   A 5 ILE A  99  ASP A 104 -1  O  LEU A 101   N  LYS A  48           
SHEET    5   A 5 LEU A  81  CYS A  85 -1  N  CYS A  85   O  TYR A 100           
SHEET    1   B 3 HIS A 108  ASP A 109  0                                        
SHEET    2   B 3 VAL A 155  ILE A 157 -1  O  ILE A 157   N  HIS A 108           
SHEET    3   B 3 LEU A 163  LEU A 165 -1  O  LYS A 164   N  LEU A 156           
SHEET    1   C 2 ILE A 145  LEU A 146  0                                        
SHEET    2   C 2 ARG A 172  ALA A 173 -1  O  ARG A 172   N  LEU A 146           
LINK         C   TYR A 185                 N   TPO A 186     1555   1555  1.33  
LINK         C   TPO A 186                 N   ASN A 187     1555   1555  1.33  
CISPEP   1 ASP A  318    PRO A  319          0        -2.15                     
SITE     1 AC1  2 ASN A 154  ASP A 167                                          
SITE     1 AC2 10 GLN A  27  ALA A  46  LYS A  48  PHE A 103                    
SITE     2 AC2 10 ASP A 104  CYS A 106  ASP A 149  LYS A 151                    
SITE     3 AC2 10 ASN A 154  ASP A 167                                          
SITE     1 AC3  6 GLN B  46  GLN B  56  THR B 179  ARG B 254                    
SITE     2 AC3  6 HOH B 271  HOH B 276                                          
CRYST1  173.130  173.130   95.640  90.00  90.00 120.00 H 3           9          
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      0.005776  0.003335  0.000000        0.00000                         
SCALE2      0.000000  0.006670  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010456        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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