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Database: PDB
Entry: 3MY5
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Original site: 3MY5 
HEADER    TRANSFERASE/PROTEIN BINDING/INHIBITOR   09-MAY-10   3MY5              
TITLE     CDK2/CYCLINA IN COMPLEX WITH DRB                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CELL DIVISION PROTEIN KINASE 2;                            
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: P33 PROTEIN KINASE;                                         
COMPND   5 EC: 2.7.11.22;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CYCLIN-A2;                                                 
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 FRAGMENT: UNP RESIDUES 169-430;                                      
COMPND  11 SYNONYM: CYCLIN-A;                                                   
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CDK2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: BOS TAURUS;                                     
SOURCE  11 ORGANISM_COMMON: BOVINE;                                             
SOURCE  12 ORGANISM_TAXID: 9913;                                                
SOURCE  13 GENE: CCNA2, CCNA;                                                   
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE  16 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    CDK, CYCLIN, INHIBITOR, DRB, TRANSFERASE-PROTEIN BINDING-INHIBITOR    
KEYWDS   2 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.BAUMLI,L.N.JOHNSON                                                  
REVDAT   2   29-JUN-11 3MY5    1       JRNL   HEADER                            
REVDAT   1   29-SEP-10 3MY5    0                                                
JRNL        AUTH   S.BAUMLI,J.A.ENDICOTT,L.N.JOHNSON                            
JRNL        TITL   HALOGEN BONDS FORM THE BASIS FOR SELECTIVE P-TEFB INHIBITION 
JRNL        TITL 2 BY DRB                                                       
JRNL        REF    CHEM.BIOL.                    V.  17   931 2010              
JRNL        REFN                   ISSN 1074-5521                               
JRNL        PMID   20851342                                                     
JRNL        DOI    10.1016/J.CHEMBIOL.2010.07.012                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.1_357)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 59.53                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.130                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 83313                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 8367                            
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 59.5502 -  6.5224    0.99     5224   272  0.1754 0.1726        
REMARK   3     2  6.5224 -  5.1780    0.97     5100   303  0.1467 0.1771        
REMARK   3     3  5.1780 -  4.5237    0.99     5239   264  0.1300 0.1902        
REMARK   3     4  4.5237 -  4.1102    1.00     5235   316  0.1215 0.1545        
REMARK   3     5  4.1102 -  3.8157    1.00     5321   263  0.1347 0.1719        
REMARK   3     6  3.8157 -  3.5907    1.00     5273   306  0.1416 0.1760        
REMARK   3     7  3.5907 -  3.4109    1.00     5245   302  0.1490 0.2122        
REMARK   3     8  3.4109 -  3.2625    1.00     5262   268  0.1582 0.1944        
REMARK   3     9  3.2625 -  3.1369    1.00     5348   237  0.1701 0.1990        
REMARK   3    10  3.1369 -  3.0286    1.00     5308   261  0.1884 0.2255        
REMARK   3    11  3.0286 -  2.9339    1.00     5264   300  0.1937 0.2287        
REMARK   3    12  2.9339 -  2.8501    1.00     5241   287  0.2102 0.2777        
REMARK   3    13  2.8501 -  2.7750    1.00     5323   261  0.1994 0.2614        
REMARK   3    14  2.7750 -  2.7073    1.00     5322   257  0.1961 0.2448        
REMARK   3    15  2.7073 -  2.6458    1.00     5217   317  0.2025 0.2638        
REMARK   3    16  2.6458 -  2.5895    1.00     5342   276  0.1942 0.2525        
REMARK   3    17  2.5895 -  2.5377    1.00     5239   303  0.1880 0.2221        
REMARK   3    18  2.5377 -  2.4898    1.00     5255   282  0.1967 0.2617        
REMARK   3    19  2.4898 -  2.4453    1.00     5347   264  0.2085 0.2666        
REMARK   3    20  2.4453 -  2.4039    1.00     5194   330  0.2096 0.2489        
REMARK   3    21  2.4039 -  2.3651    1.00     5336   270  0.2105 0.2533        
REMARK   3    22  2.3651 -  2.3287    1.00     5267   267  0.2070 0.2408        
REMARK   3    23  2.3287 -  2.2945    1.00     5276   313  0.2101 0.2353        
REMARK   3    24  2.2945 -  2.2621    1.00     5275   285  0.2201 0.2538        
REMARK   3    25  2.2621 -  2.2316    1.00     5327   248  0.2347 0.3022        
REMARK   3    26  2.2316 -  2.2026    1.00     5307   224  0.2389 0.2490        
REMARK   3    27  2.2026 -  2.1751    1.00     5300   270  0.2452 0.2521        
REMARK   3    28  2.1751 -  2.1489    1.00     5321   272  0.2431 0.2911        
REMARK   3    29  2.1489 -  2.1239    1.00     5246   268  0.2518 0.2856        
REMARK   3    30  2.1239 -  2.1000    1.00     5306   281  0.2664 0.2995        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.38                                          
REMARK   3   B_SOL              : 48.03                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.290            
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) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.11630                                             
REMARK   3    B22 (A**2) : 0.04160                                              
REMARK   3    B33 (A**2) : 1.07470                                              
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      :  0.007           9112                                  
REMARK   3   ANGLE     :  1.060          12394                                  
REMARK   3   CHIRALITY :  0.070           1418                                  
REMARK   3   PLANARITY :  0.005           1556                                  
REMARK   3   DIHEDRAL  : 14.159           3413                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: all                                                    
REMARK   3    ORIGIN FOR THE GROUP (A): -28.4355   8.0466 -17.3242              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0540 T22:   0.0435                                     
REMARK   3      T33:   0.0421 T12:   0.0164                                     
REMARK   3      T13:   0.0169 T23:  -0.0074                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2830 L22:   0.2933                                     
REMARK   3      L33:   0.3163 L12:   0.1151                                     
REMARK   3      L13:   0.1112 L23:   0.2140                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0055 S12:  -0.0766 S13:   0.0345                       
REMARK   3      S21:  -0.0163 S22:  -0.0500 S23:   0.0038                       
REMARK   3      S31:   0.0487 S32:  -0.0024 S33:   0.0386                       
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 3MY5 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 20-MAY-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB059140.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-MAY-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID14-4                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : SINGLE SILICON (111)               
REMARK 200                                   MONOCHROMATOR AND TOROIDAL         
REMARK 200                                   FOCUSING MIRROR                    
REMARK 200  OPTICS                         : SINGLE SILICON (111)               
REMARK 200                                   MONOCHROMATOR AND TOROIDAL         
REMARK 200                                   FOCUSING MIRROR                    
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 87151                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 59.550                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.000                              
REMARK 200  R MERGE                    (I) : 0.09800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 4.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.59500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.600                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3BHT, OMITTING THE INHIBITOR               
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.1M AMMONIUM SULPHATE, 100MM HEPES PH   
REMARK 280  7.0, 5MM DTT, SATURATED DRB, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       37.13000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       74.20500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       67.13000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       74.20500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.13000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       67.13000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: 3570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23560 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 3630 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22450 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
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     ASP A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     GLU A    40                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     THR C   221                                                      
REMARK 465     PRO C   222                                                      
REMARK 465     ASP C   223                                                      
REMARK 465     GLU C   224                                                      
REMARK 465     VAL C   225                                                      
REMARK 465     VAL C   226                                                      
REMARK 465     TRP C   227                                                      
REMARK 465     PRO C   228                                                      
REMARK 465     GLY C   229                                                      
REMARK 465     VAL C   230                                                      
REMARK 465     THR C   231                                                      
REMARK 465     SER C   232                                                      
REMARK 465     MET C   233                                                      
REMARK 465     PRO C   234                                                      
REMARK 465     ASP C   235                                                      
REMARK 465     TYR C   236                                                      
REMARK 465     LYS C   237                                                      
REMARK 465     PRO C   238                                                      
REMARK 465     SER C   239                                                      
REMARK 465     PHE C   240                                                      
REMARK 465     PRO C   241                                                      
REMARK 465     LYS C   242                                                      
REMARK 465     TRP C   243                                                      
REMARK 465     ALA C   244                                                      
REMARK 465     ARG C   245                                                      
REMARK 465     GLN C   246                                                      
REMARK 465     ASP C   247                                                      
REMARK 465     PHE C   248                                                      
REMARK 465     SER C   249                                                      
REMARK 465     LYS C   250                                                      
REMARK 465     ARG C   297                                                      
REMARK 465     LEU C   298                                                      
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    HOH A   469     O    HOH A   471              2.18            
REMARK 500   OD1  ASP A   210     O    HOH A   470              2.19            
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    HIS A  71       72.00   -119.47                                   
REMARK 500    THR A  72     -178.03    -55.12                                   
REMARK 500    LEU A  96      -12.84     68.47                                   
REMARK 500    ASP A 127       41.69   -152.10                                   
REMARK 500    ASP A 145       76.52     53.60                                   
REMARK 500    VAL A 164      127.46     76.12                                   
REMARK 500    SER A 181     -155.41   -144.05                                   
REMARK 500    VAL B 175       64.58     31.07                                   
REMARK 500    TRP B 372      111.66    -33.04                                   
REMARK 500    THR C  14      -13.51   -152.60                                   
REMARK 500    THR C  41      -74.92   -136.74                                   
REMARK 500    ASP C 127       44.25   -155.19                                   
REMARK 500    ASP C 145       71.36     49.57                                   
REMARK 500    VAL C 164      122.72     70.99                                   
REMARK 500    SER C 181     -159.66   -144.58                                   
REMARK 500    PRO C 254        0.36    -65.13                                   
REMARK 500    THR C 290     -162.05   -126.21                                   
REMARK 500    ASP D 283     -128.82     55.28                                   
REMARK 500    TRP D 372      107.22    -51.00                                   
REMARK 500    LYS D 417      -36.77    -39.51                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B 437        DISTANCE =  6.17 ANGSTROMS                       
REMARK 525    HOH C 535        DISTANCE =  5.04 ANGSTROMS                       
REMARK 525    HOH D 475        DISTANCE =  5.22 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RFZ A 300                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGM B 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FMT B 2                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RFZ C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SGM D 2                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3MY1   RELATED DB: PDB                                   
DBREF  3MY5 A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  3MY5 B  171   432  UNP    P30274   CCNA2_BOVIN    169    430             
DBREF  3MY5 C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  3MY5 D  171   432  UNP    P30274   CCNA2_BOVIN    169    430             
SEQADV 3MY5 GLY A   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 3MY5 SER A    0  UNP  P24941              EXPRESSION TAG                 
SEQADV 3MY5 GLY C   -1  UNP  P24941              EXPRESSION TAG                 
SEQADV 3MY5 SER C    0  UNP  P24941              EXPRESSION TAG                 
SEQRES   1 A  300  GLY SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY          
SEQRES   2 A  300  GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS          
SEQRES   3 A  300  LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU          
SEQRES   4 A  300  ASP THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG          
SEQRES   5 A  300  GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE          
SEQRES   6 A  300  VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU          
SEQRES   7 A  300  TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS          
SEQRES   8 A  300  PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO          
SEQRES   9 A  300  LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU          
SEQRES  10 A  300  ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU          
SEQRES  11 A  300  LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE          
SEQRES  12 A  300  LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL          
SEQRES  13 A  300  PRO VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP          
SEQRES  14 A  300  TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR          
SEQRES  15 A  300  SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE          
SEQRES  16 A  300  ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP          
SEQRES  17 A  300  SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU          
SEQRES  18 A  300  GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER          
SEQRES  19 A  300  MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG          
SEQRES  20 A  300  GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP          
SEQRES  21 A  300  GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO          
SEQRES  22 A  300  ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO          
SEQRES  23 A  300  PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG          
SEQRES  24 A  300  LEU                                                          
SEQRES   1 B  262  SER VAL ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS          
SEQRES   2 B  262  THR TYR LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS          
SEQRES   3 B  262  VAL GLY TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER          
SEQRES   4 B  262  MET ARG ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY          
SEQRES   5 B  262  GLU GLU TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA          
SEQRES   6 B  262  VAL ASN TYR ILE ASP ARG PHE LEU SER SER MET SER VAL          
SEQRES   7 B  262  LEU ARG GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET          
SEQRES   8 B  262  LEU LEU ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU          
SEQRES   9 B  262  VAL ALA GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR          
SEQRES  10 B  262  LYS LYS GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS          
SEQRES  11 B  262  VAL LEU ALA PHE ASP LEU ALA ALA PRO THR ILE ASN GLN          
SEQRES  12 B  262  PHE LEU THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN          
SEQRES  13 B  262  CYS LYS VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU          
SEQRES  14 B  262  SER LEU ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO          
SEQRES  15 B  262  SER VAL ILE ALA ALA ALA ALA PHE HIS LEU ALA LEU TYR          
SEQRES  16 B  262  THR VAL THR GLY GLN SER TRP PRO GLU SER LEU VAL GLN          
SEQRES  17 B  262  LYS THR GLY TYR THR LEU GLU THR LEU LYS PRO CYS LEU          
SEQRES  18 B  262  LEU ASP LEU HIS GLN THR TYR LEU ARG ALA PRO GLN HIS          
SEQRES  19 B  262  ALA GLN GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS          
SEQRES  20 B  262  TYR HIS GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU          
SEQRES  21 B  262  ASN VAL                                                      
SEQRES   1 C  300  GLY SER MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY          
SEQRES   2 C  300  GLU GLY THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS          
SEQRES   3 C  300  LEU THR GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU          
SEQRES   4 C  300  ASP THR GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG          
SEQRES   5 C  300  GLU ILE SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE          
SEQRES   6 C  300  VAL LYS LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU          
SEQRES   7 C  300  TYR LEU VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS          
SEQRES   8 C  300  PHE MET ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO          
SEQRES   9 C  300  LEU ILE LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU          
SEQRES  10 C  300  ALA PHE CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU          
SEQRES  11 C  300  LYS PRO GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE          
SEQRES  12 C  300  LYS LEU ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL          
SEQRES  13 C  300  PRO VAL ARG THR TYR TPO HIS GLU VAL VAL THR LEU TRP          
SEQRES  14 C  300  TYR ARG ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR          
SEQRES  15 C  300  SER THR ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE          
SEQRES  16 C  300  ALA GLU MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP          
SEQRES  17 C  300  SER GLU ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU          
SEQRES  18 C  300  GLY THR PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER          
SEQRES  19 C  300  MET PRO ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG          
SEQRES  20 C  300  GLN ASP PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP          
SEQRES  21 C  300  GLY ARG SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO          
SEQRES  22 C  300  ASN LYS ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO          
SEQRES  23 C  300  PHE PHE GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG          
SEQRES  24 C  300  LEU                                                          
SEQRES   1 D  262  SER VAL ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS          
SEQRES   2 D  262  THR TYR LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS          
SEQRES   3 D  262  VAL GLY TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER          
SEQRES   4 D  262  MET ARG ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY          
SEQRES   5 D  262  GLU GLU TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA          
SEQRES   6 D  262  VAL ASN TYR ILE ASP ARG PHE LEU SER SER MET SER VAL          
SEQRES   7 D  262  LEU ARG GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET          
SEQRES   8 D  262  LEU LEU ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU          
SEQRES   9 D  262  VAL ALA GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR          
SEQRES  10 D  262  LYS LYS GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS          
SEQRES  11 D  262  VAL LEU ALA PHE ASP LEU ALA ALA PRO THR ILE ASN GLN          
SEQRES  12 D  262  PHE LEU THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN          
SEQRES  13 D  262  CYS LYS VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU          
SEQRES  14 D  262  SER LEU ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO          
SEQRES  15 D  262  SER VAL ILE ALA ALA ALA ALA PHE HIS LEU ALA LEU TYR          
SEQRES  16 D  262  THR VAL THR GLY GLN SER TRP PRO GLU SER LEU VAL GLN          
SEQRES  17 D  262  LYS THR GLY TYR THR LEU GLU THR LEU LYS PRO CYS LEU          
SEQRES  18 D  262  LEU ASP LEU HIS GLN THR TYR LEU ARG ALA PRO GLN HIS          
SEQRES  19 D  262  ALA GLN GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS          
SEQRES  20 D  262  TYR HIS GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU          
SEQRES  21 D  262  ASN VAL                                                      
MODRES 3MY5 TPO A  160  THR  PHOSPHOTHREONINE                                   
MODRES 3MY5 TPO C  160  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 160      11                                                       
HET    TPO  C 160      11                                                       
HET    RFZ  A 300      20                                                       
HET    FMT  A 301       3                                                       
HET    SGM  B   1       6                                                       
HET    FMT  B   2       3                                                       
HET    FMT  B   3       3                                                       
HET    RFZ  C 301      20                                                       
HET    SGM  D   2       6                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     RFZ 5,6-DICHLORO-1-BETA-D-RIBOFURANOSYL-1H-BENZIMIDAZOLE             
HETNAM     FMT FORMIC ACID                                                      
HETNAM     SGM MONOTHIOGLYCEROL                                                 
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    2(C4 H10 N O6 P)                                             
FORMUL   5  RFZ    2(C12 H12 CL2 N2 O4)                                         
FORMUL   6  FMT    3(C H2 O2)                                                   
FORMUL   7  SGM    2(C3 H8 O2 S)                                                
FORMUL  12  HOH   *526(H2 O)                                                    
HELIX    1   1 SER A    0  GLU A    2  5                                   3    
HELIX    2   2 PRO A   45  LYS A   56  1                                  12    
HELIX    3   3 LEU A   87  SER A   94  1                                   8    
HELIX    4   4 PRO A  100  HIS A  121  1                                  22    
HELIX    5   5 LYS A  129  GLN A  131  5                                   3    
HELIX    6   6 THR A  165  ARG A  169  5                                   5    
HELIX    7   7 ALA A  170  LEU A  175  1                                   6    
HELIX    8   8 THR A  182  ARG A  199  1                                  18    
HELIX    9   9 SER A  207  GLY A  220  1                                  14    
HELIX   10  10 GLY A  229  MET A  233  5                                   5    
HELIX   11  11 ASP A  247  VAL A  251  5                                   5    
HELIX   12  12 ASP A  256  LEU A  267  1                                  12    
HELIX   13  13 SER A  276  LEU A  281  1                                   6    
HELIX   14  14 ALA A  282  GLN A  287  5                                   6    
HELIX   15  15 SER B  171  VAL B  175  5                                   5    
HELIX   16  16 TYR B  178  CYS B  193  1                                  16    
HELIX   17  17 GLY B  198  GLN B  203  1                                   6    
HELIX   18  18 THR B  207  LYS B  226  1                                  20    
HELIX   19  19 GLN B  228  MET B  246  1                                  19    
HELIX   20  20 LEU B  249  GLY B  251  5                                   3    
HELIX   21  21 LYS B  252  GLU B  269  1                                  18    
HELIX   22  22 GLU B  274  THR B  282  1                                   9    
HELIX   23  23 THR B  287  ALA B  303  1                                  17    
HELIX   24  24 THR B  310  LEU B  320  1                                  11    
HELIX   25  25 ASN B  326  ASP B  343  1                                  18    
HELIX   26  26 ASP B  343  LEU B  348  1                                   6    
HELIX   27  27 LEU B  351  GLY B  369  1                                  19    
HELIX   28  28 PRO B  373  GLY B  381  1                                   9    
HELIX   29  29 THR B  383  ALA B  401  1                                  19    
HELIX   30  30 PRO B  402  HIS B  404  5                                   3    
HELIX   31  31 GLN B  407  TYR B  413  1                                   7    
HELIX   32  32 LYS B  414  HIS B  419  5                                   6    
HELIX   33  33 GLY B  420  LEU B  424  5                                   5    
HELIX   34  34 PRO C   45  LEU C   58  1                                  14    
HELIX   35  35 LEU C   87  SER C   94  1                                   8    
HELIX   36  36 PRO C  100  HIS C  121  1                                  22    
HELIX   37  37 LYS C  129  GLN C  131  5                                   3    
HELIX   38  38 ASP C  145  ALA C  149  5                                   5    
HELIX   39  39 THR C  165  ARG C  169  5                                   5    
HELIX   40  40 ALA C  170  LEU C  175  1                                   6    
HELIX   41  41 THR C  182  ARG C  199  1                                  18    
HELIX   42  42 SER C  207  LEU C  219  1                                  13    
HELIX   43  43 ASP C  256  LEU C  267  1                                  12    
HELIX   44  44 SER C  276  LEU C  281  1                                   6    
HELIX   45  45 ALA C  282  GLN C  287  5                                   6    
HELIX   46  46 SER D  171  VAL D  175  5                                   5    
HELIX   47  47 TYR D  178  CYS D  193  1                                  16    
HELIX   48  48 GLY D  198  GLN D  203  1                                   6    
HELIX   49  49 THR D  207  TYR D  225  1                                  19    
HELIX   50  50 GLN D  228  MET D  246  1                                  19    
HELIX   51  51 LEU D  249  GLY D  251  5                                   3    
HELIX   52  52 LYS D  252  GLU D  269  1                                  18    
HELIX   53  53 GLU D  274  THR D  282  1                                   9    
HELIX   54  54 THR D  287  LEU D  302  1                                  16    
HELIX   55  55 THR D  310  PHE D  319  1                                  10    
HELIX   56  56 LEU D  320  GLN D  322  5                                   3    
HELIX   57  57 ASN D  326  ASP D  343  1                                  18    
HELIX   58  58 ASP D  343  LEU D  348  1                                   6    
HELIX   59  59 LEU D  351  THR D  368  1                                  18    
HELIX   60  60 PRO D  373  GLY D  381  1                                   9    
HELIX   61  61 LEU D  387  ALA D  401  1                                  15    
HELIX   62  62 PRO D  402  HIS D  404  5                                   3    
HELIX   63  63 GLN D  407  TYR D  413  1                                   7    
HELIX   64  64 LYS D  414  HIS D  419  5                                   6    
HELIX   65  65 GLY D  420  LEU D  424  5                                   5    
SHEET    1   A 5 PHE A   4  GLU A  12  0                                        
SHEET    2   A 5 VAL A  17  ASN A  23 -1  O  LYS A  20   N  VAL A   7           
SHEET    3   A 5 VAL A  29  ARG A  36 -1  O  LEU A  32   N  TYR A  19           
SHEET    4   A 5 LYS A  75  GLU A  81 -1  O  LEU A  76   N  ILE A  35           
SHEET    5   A 5 LEU A  66  HIS A  71 -1  N  LEU A  67   O  VAL A  79           
SHEET    1   B 3 GLN A  85  ASP A  86  0                                        
SHEET    2   B 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3   B 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1   C 2 VAL A 123  LEU A 124  0                                        
SHEET    2   C 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1   D 5 PHE C   4  GLU C  12  0                                        
SHEET    2   D 5 VAL C  17  ASN C  23 -1  O  VAL C  18   N  ILE C  10           
SHEET    3   D 5 VAL C  29  ARG C  36 -1  O  LEU C  32   N  TYR C  19           
SHEET    4   D 5 LYS C  75  GLU C  81 -1  O  LEU C  76   N  ILE C  35           
SHEET    5   D 5 LEU C  66  HIS C  71 -1  N  LEU C  67   O  VAL C  79           
SHEET    1   E 3 GLN C  85  ASP C  86  0                                        
SHEET    2   E 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  GLN C  85           
SHEET    3   E 3 ILE C 141  LEU C 143 -1  O  LYS C 142   N  LEU C 134           
SHEET    1   F 2 VAL C 123  LEU C 124  0                                        
SHEET    2   F 2 ARG C 150  ALA C 151 -1  O  ARG C 150   N  LEU C 124           
LINK         C   TYR A 159                 N   TPO A 160     1555   1555  1.32  
LINK         C   TPO A 160                 N   HIS A 161     1555   1555  1.33  
LINK         C   TYR C 159                 N   TPO C 160     1555   1555  1.33  
LINK         C   TPO C 160                 N   HIS C 161     1555   1555  1.33  
CISPEP   1 THR A   14    TYR A   15          0         8.82                     
CISPEP   2 TYR A   15    GLY A   16          0         1.77                     
CISPEP   3 VAL A  154    PRO A  155          0        -3.32                     
CISPEP   4 GLN B  323    PRO B  324          0        -1.76                     
CISPEP   5 ASP B  345    PRO B  346          0         8.74                     
CISPEP   6 VAL C  154    PRO C  155          0        -3.80                     
CISPEP   7 GLN D  323    PRO D  324          0        -2.78                     
CISPEP   8 ASP D  345    PRO D  346          0        10.04                     
SITE     1 AC1 13 ILE A  10  GLU A  12  VAL A  18  ALA A  31                    
SITE     2 AC1 13 LYS A  33  GLU A  81  LEU A  83  GLN A 131                    
SITE     3 AC1 13 LEU A 134  HOH A 394  HOH A 453  HOH A 488                    
SITE     4 AC1 13 HOH A 499                                                     
SITE     1 AC2  4 VAL A 226  HIS A 268  TYR A 269  HOH A 306                    
SITE     1 AC3  4 LYS B 192  CYS B 193  ARG B 241  ASP B 305                    
SITE     1 AC4  5 THR A 182  SER A 276  VAL B 175  PRO B 176                    
SITE     2 AC4  5 ASP B 177                                                     
SITE     1 AC5  8 ILE C  10  ALA C  31  GLU C  81  ASP C  86                    
SITE     2 AC5  8 GLN C 131  ASN C 132  LEU C 134  ASP C 145                    
SITE     1 AC6  3 CYS D 193  ARG D 241  ASP D 305                               
CRYST1   74.260  134.260  148.410  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013466  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007448  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006738        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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