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Database: PDB
Entry: 2I40
LinkDB: 2I40
Original site: 2I40 
HEADER    TRANSFERASE/CELL CYCLE                  21-AUG-06   2I40              
TITLE     CDK2/CYCLIN A COMPLEXED WITH A THIOPHENE CARBOXAMIDE INHIBITOR        
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: RESIDUES 173-432;                                          
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: 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: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PFASTBAC;                                 
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 GENE: CCNA2, CCN1, CCNA;                                             
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  19 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  20 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID                               
KEYWDS    CDK2, CYCLIN, KINASE, TRANSFERASE-CELL CYCLE COMPLEX                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.M.SHEWCHUK                                                          
REVDAT   4   13-JUL-11 2I40    1       VERSN                                    
REVDAT   3   24-FEB-09 2I40    1       VERSN                                    
REVDAT   2   05-DEC-06 2I40    1       JRNL                                     
REVDAT   1   10-OCT-06 2I40    0                                                
JRNL        AUTH   P.BAMBOROUGH,J.A.CHRISTOPHER,G.J.CUTLER,M.C.DICKSON,         
JRNL        AUTH 2 G.W.MELLOR,J.V.MOREY,C.B.PATEL,L.M.SHEWCHUK                  
JRNL        TITL   5-(1H-BENZIMIDAZOL-1-YL)-3-ALKOXY-2-THIOPHENECARBONITRILES   
JRNL        TITL 2 AS POTENT, SELECTIVE, INHIBITORS OF IKK-EPSILON KINASE       
JRNL        REF    BIOORG.MED.CHEM.LETT.         V.  16  6236 2006              
JRNL        REFN                   ISSN 0960-894X                               
JRNL        PMID   16997559                                                     
JRNL        DOI    10.1016/J.BMCL.2006.09.018                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 160.13                         
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 48311                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2579                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.87                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2695                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 73.07                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2740                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 130                          
REMARK   3   BIN FREE R VALUE                    : 0.3030                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8772                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 62                                      
REMARK   3   SOLVENT ATOMS            : 242                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 73.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 63.45                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.94000                                              
REMARK   3    B22 (A**2) : 1.94000                                              
REMARK   3    B33 (A**2) : -2.91000                                             
REMARK   3    B12 (A**2) : 0.97000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.490         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.279         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.200         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.005        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9096 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12370 ; 1.120 ; 1.985       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1105 ; 5.086 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   379 ;39.289 ;23.984       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1580 ;14.279 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    41 ;19.750 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1404 ; 0.077 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6865 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4250 ; 0.188 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  6279 ; 0.304 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   383 ; 0.139 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    46 ; 0.217 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.144 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5665 ; 0.336 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8972 ; 0.591 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3934 ; 0.828 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3393 ; 1.389 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 5                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : B D                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     B    180       B     425      2                      
REMARK   3           1     D    180       D     425      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    B    (A):    980 ;  0.03 ;  0.05           
REMARK   3   MEDIUM POSITIONAL  1    B    (A):    987 ;  0.40 ;  0.50           
REMARK   3   TIGHT THERMAL      1    B (A**2):    980 ;  0.04 ;  0.50           
REMARK   3   MEDIUM THERMAL     1    B (A**2):    987 ;  0.30 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     85       A     140      4                      
REMARK   3           1     C     85       C     140      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):    427 ;  0.18 ;  0.50           
REMARK   3   MEDIUM THERMAL     2    A (A**2):    427 ;  0.33 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     10       A      83      4                      
REMARK   3           1     C     10       C      83      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  3    A    (A):    526 ;  0.43 ;  0.50           
REMARK   3   MEDIUM THERMAL     3    A (A**2):    526 ;  0.26 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : A C                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    170       A     280      4                      
REMARK   3           1     C    170       C     280      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  4    A    (A):    874 ;  0.23 ;  0.50           
REMARK   3   MEDIUM THERMAL     4    A (A**2):    874 ;  0.23 ;  2.00           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 5                                  
REMARK   3     CHAIN NAMES                    : C A                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     C    401       C     401      4                      
REMARK   3           1     A    301       A     301      4                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  5    C    (A):     31 ;  0.06 ;  0.50           
REMARK   3   MEDIUM THERMAL     5    C (A**2):     31 ;  0.54 ;  2.00           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    84                          
REMARK   3    ORIGIN FOR THE GROUP (A): -16.4282 199.3437 108.1834              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0997 T22:   0.0867                                     
REMARK   3      T33:  -0.1682 T12:  -0.0626                                     
REMARK   3      T13:   0.1033 T23:  -0.1373                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.3280 L22:   2.7985                                     
REMARK   3      L33:   1.9173 L12:  -0.9261                                     
REMARK   3      L13:  -2.0275 L23:   1.2074                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1505 S12:  -0.8551 S13:  -0.5675                       
REMARK   3      S21:   0.4428 S22:  -0.0894 S23:  -0.0139                       
REMARK   3      S31:   0.4953 S32:   0.3590 S33:   0.2399                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     1        C    84                          
REMARK   3    ORIGIN FOR THE GROUP (A): -28.5581 178.5651  90.2927              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1477 T22:  -0.0260                                     
REMARK   3      T33:   0.1116 T12:  -0.1094                                     
REMARK   3      T13:   0.2256 T23:  -0.1558                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6954 L22:   2.6732                                     
REMARK   3      L33:   6.6970 L12:   1.0516                                     
REMARK   3      L13:  -2.1637 L23:  -2.1805                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3880 S12:  -0.1806 S13:  -0.6905                       
REMARK   3      S21:  -0.0970 S22:  -0.2158 S23:  -0.4566                       
REMARK   3      S31:   0.8040 S32:   0.5560 S33:   0.6038                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    85        A   297                          
REMARK   3    ORIGIN FOR THE GROUP (A): -21.5091 221.9416 122.5995              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2387 T22:  -0.1232                                     
REMARK   3      T33:  -0.2805 T12:  -0.0311                                     
REMARK   3      T13:   0.0200 T23:  -0.1054                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1170 L22:   1.8140                                     
REMARK   3      L33:   3.5930 L12:   0.8038                                     
REMARK   3      L13:  -0.2436 L23:   0.9396                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0003 S12:  -0.1976 S13:   0.2046                       
REMARK   3      S21:   0.1611 S22:  -0.1831 S23:   0.1287                       
REMARK   3      S31:  -0.1179 S32:  -0.1838 S33:   0.1828                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C    85        C   296                          
REMARK   3    ORIGIN FOR THE GROUP (A): -41.3273 176.0477  65.7117              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0186 T22:  -0.1505                                     
REMARK   3      T33:   0.0875 T12:  -0.0386                                     
REMARK   3      T13:   0.0080 T23:  -0.2756                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4378 L22:   3.4989                                     
REMARK   3      L33:   4.4023 L12:  -0.1083                                     
REMARK   3      L13:  -0.1923 L23:   1.1147                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1705 S12:  -0.0318 S13:  -0.0599                       
REMARK   3      S21:  -0.1937 S22:  -0.2922 S23:   0.6400                       
REMARK   3      S31:   0.5574 S32:  -0.2740 S33:   0.1218                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   175        B   431                          
REMARK   3    ORIGIN FOR THE GROUP (A): -48.6624 199.6286 112.5400              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2009 T22:   0.0279                                     
REMARK   3      T33:  -0.2363 T12:  -0.0996                                     
REMARK   3      T13:   0.1452 T23:  -0.1840                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4815 L22:   3.0553                                     
REMARK   3      L33:   2.3334 L12:  -1.0429                                     
REMARK   3      L13:  -0.6577 L23:   0.1371                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2368 S12:  -0.0290 S13:  -0.1770                       
REMARK   3      S21:   0.3189 S22:  -0.0370 S23:   0.2145                       
REMARK   3      S31:   0.1524 S32:  -0.2134 S33:   0.2738                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   D   178        D   432                          
REMARK   3    ORIGIN FOR THE GROUP (A): -19.9284 204.5111  72.7158              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2295 T22:  -0.2595                                     
REMARK   3      T33:  -0.1377 T12:  -0.0241                                     
REMARK   3      T13:   0.0796 T23:  -0.1574                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1668 L22:   2.2768                                     
REMARK   3      L33:   3.7755 L12:  -0.4003                                     
REMARK   3      L13:  -0.0016 L23:  -0.8588                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0019 S12:   0.1108 S13:   0.1188                       
REMARK   3      S21:  -0.0505 S22:  -0.2075 S23:   0.3576                       
REMARK   3      S31:  -0.0360 S32:  -0.0561 S33:   0.2094                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2I40 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 22-AUG-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB039108.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUL-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 93                                 
REMARK 200  PH                             : 6.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
REMARK 200  MONOCHROMATOR                  : MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 48311                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 160.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY                : 8.400                              
REMARK 200  R MERGE                    (I) : 0.11000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 40.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.87                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 73.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.47000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.780                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: PDB ENTRY 1FIN                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.11                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M SODIUM ACETATE, 100 MM SODIUM      
REMARK 280  CACODYLATE, PH 6.7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE      
REMARK 280  277K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 62 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+2/3                                            
REMARK 290       3555   -X+Y,-X,Z+1/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+2/3                                            
REMARK 290       6555   X-Y,X,Z+1/3                                             
REMARK 290       7555   Y,X,-Z+2/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+1/3                                          
REMARK 290      10555   -Y,-X,-Z+2/3                                            
REMARK 290      11555   -X+Y,Y,-Z                                               
REMARK 290      12555   X,X-Y,-Z+1/3                                            
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      142.00000            
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       71.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      142.00000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       71.00000            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000      142.00000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       71.00000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      142.00000            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       71.00000            
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 300 REMARK: 2 CDK2/CYCLINA HETERODIMERS PER ASU                          
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: 3900 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23930 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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: 3690 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23620 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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     THR A   160                                                      
REMARK 465     HIS A   161                                                      
REMARK 465     GLU A   162                                                      
REMARK 465     LEU A   298                                                      
REMARK 465     ASN B   173                                                      
REMARK 465     GLU B   174                                                      
REMARK 465     LEU B   432                                                      
REMARK 465     ARG C   297                                                      
REMARK 465     LEU C   298                                                      
REMARK 465     ASN D   173                                                      
REMARK 465     GLU D   174                                                      
REMARK 465     VAL D   175                                                      
REMARK 465     PRO D   176                                                      
REMARK 465     ASP D   177                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A   2    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  12    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  36    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     HIS A  71    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG A 157    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR A 159    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN B 323    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 378    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C  75    CG   CD   CE   NZ                                   
REMARK 470     LEU C  96    CG   CD1  CD2                                       
REMARK 470     GLU C 162    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 200    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN C 287    CG   CD   OE1  NE2                                  
REMARK 470     HIS C 295    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LEU C 296    CG   CD1  CD2                                       
REMARK 470     TYR D 178    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN D 323    CG   CD   OE1  NE2                                  
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   SG   CYS B   193     O    HOH B   478              1.96            
REMARK 500   OH   TYR B   199     OD1  ASP B   240              2.07            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  42       -9.50   -140.16                                   
REMARK 500    ARG A 126      -11.69     80.86                                   
REMARK 500    ASP A 145       74.51     54.65                                   
REMARK 500    PHE A 146       33.14    -89.47                                   
REMARK 500    ASP A 223     -169.27   -122.53                                   
REMARK 500    PHE B 304        9.47     57.70                                   
REMARK 500    TRP B 372      107.29    -32.52                                   
REMARK 500    VAL C   7      -61.93    -97.57                                   
REMARK 500    LEU C  37      118.00     64.41                                   
REMARK 500    LEU C  58       77.82   -101.41                                   
REMARK 500    ARG C 126      -19.08     84.43                                   
REMARK 500    ASP C 145       77.51     51.55                                   
REMARK 500    PRO C 284      -26.92    -39.07                                   
REMARK 500    PHE D 304       13.85     57.91                                   
REMARK 500    TRP D 372      109.88    -36.08                                   
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 BLZ A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BLZ C 401                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1FIN   RELATED DB: PDB                                   
DBREF  2I40 A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  2I40 C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  2I40 B  173   432  UNP    P20248   CCNA2_HUMAN    173    432             
DBREF  2I40 D  173   432  UNP    P20248   CCNA2_HUMAN    173    432             
SEQRES   1 A  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 A  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 A  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 A  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 A  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 A  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 A  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 A  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 A  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 A  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 A  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 A  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 A  298  ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 A  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 A  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 A  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 A  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 A  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 A  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 A  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 A  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 A  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 A  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
SEQRES   1 B  260  ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR          
SEQRES   2 B  260  LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY          
SEQRES   3 B  260  TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG          
SEQRES   4 B  260  ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU          
SEQRES   5 B  260  TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN          
SEQRES   6 B  260  TYR ILE ASP ARG PHE LEU SER SER MET SER VAL LEU ARG          
SEQRES   7 B  260  GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU          
SEQRES   8 B  260  ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA          
SEQRES   9 B  260  GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS          
SEQRES  10 B  260  GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU          
SEQRES  11 B  260  THR PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU          
SEQRES  12 B  260  THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS          
SEQRES  13 B  260  VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU          
SEQRES  14 B  260  ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL          
SEQRES  15 B  260  ILE ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL          
SEQRES  16 B  260  THR GLY GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR          
SEQRES  17 B  260  GLY TYR THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP          
SEQRES  18 B  260  LEU HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN          
SEQRES  19 B  260  GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS          
SEQRES  20 B  260  GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU          
SEQRES   1 C  298  MET GLU ASN PHE GLN LYS VAL GLU LYS ILE GLY GLU GLY          
SEQRES   2 C  298  THR TYR GLY VAL VAL TYR LYS ALA ARG ASN LYS LEU THR          
SEQRES   3 C  298  GLY GLU VAL VAL ALA LEU LYS LYS ILE ARG LEU ASP THR          
SEQRES   4 C  298  GLU THR GLU GLY VAL PRO SER THR ALA ILE ARG GLU ILE          
SEQRES   5 C  298  SER LEU LEU LYS GLU LEU ASN HIS PRO ASN ILE VAL LYS          
SEQRES   6 C  298  LEU LEU ASP VAL ILE HIS THR GLU ASN LYS LEU TYR LEU          
SEQRES   7 C  298  VAL PHE GLU PHE LEU HIS GLN ASP LEU LYS LYS PHE MET          
SEQRES   8 C  298  ASP ALA SER ALA LEU THR GLY ILE PRO LEU PRO LEU ILE          
SEQRES   9 C  298  LYS SER TYR LEU PHE GLN LEU LEU GLN GLY LEU ALA PHE          
SEQRES  10 C  298  CYS HIS SER HIS ARG VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  11 C  298  GLN ASN LEU LEU ILE ASN THR GLU GLY ALA ILE LYS LEU          
SEQRES  12 C  298  ALA ASP PHE GLY LEU ALA ARG ALA PHE GLY VAL PRO VAL          
SEQRES  13 C  298  ARG THR TYR THR HIS GLU VAL VAL THR LEU TRP TYR ARG          
SEQRES  14 C  298  ALA PRO GLU ILE LEU LEU GLY CYS LYS TYR TYR SER THR          
SEQRES  15 C  298  ALA VAL ASP ILE TRP SER LEU GLY CYS ILE PHE ALA GLU          
SEQRES  16 C  298  MET VAL THR ARG ARG ALA LEU PHE PRO GLY ASP SER GLU          
SEQRES  17 C  298  ILE ASP GLN LEU PHE ARG ILE PHE ARG THR LEU GLY THR          
SEQRES  18 C  298  PRO ASP GLU VAL VAL TRP PRO GLY VAL THR SER MET PRO          
SEQRES  19 C  298  ASP TYR LYS PRO SER PHE PRO LYS TRP ALA ARG GLN ASP          
SEQRES  20 C  298  PHE SER LYS VAL VAL PRO PRO LEU ASP GLU ASP GLY ARG          
SEQRES  21 C  298  SER LEU LEU SER GLN MET LEU HIS TYR ASP PRO ASN LYS          
SEQRES  22 C  298  ARG ILE SER ALA LYS ALA ALA LEU ALA HIS PRO PHE PHE          
SEQRES  23 C  298  GLN ASP VAL THR LYS PRO VAL PRO HIS LEU ARG LEU              
SEQRES   1 D  260  ASN GLU VAL PRO ASP TYR HIS GLU ASP ILE HIS THR TYR          
SEQRES   2 D  260  LEU ARG GLU MET GLU VAL LYS CYS LYS PRO LYS VAL GLY          
SEQRES   3 D  260  TYR MET LYS LYS GLN PRO ASP ILE THR ASN SER MET ARG          
SEQRES   4 D  260  ALA ILE LEU VAL ASP TRP LEU VAL GLU VAL GLY GLU GLU          
SEQRES   5 D  260  TYR LYS LEU GLN ASN GLU THR LEU HIS LEU ALA VAL ASN          
SEQRES   6 D  260  TYR ILE ASP ARG PHE LEU SER SER MET SER VAL LEU ARG          
SEQRES   7 D  260  GLY LYS LEU GLN LEU VAL GLY THR ALA ALA MET LEU LEU          
SEQRES   8 D  260  ALA SER LYS PHE GLU GLU ILE TYR PRO PRO GLU VAL ALA          
SEQRES   9 D  260  GLU PHE VAL TYR ILE THR ASP ASP THR TYR THR LYS LYS          
SEQRES  10 D  260  GLN VAL LEU ARG MET GLU HIS LEU VAL LEU LYS VAL LEU          
SEQRES  11 D  260  THR PHE ASP LEU ALA ALA PRO THR VAL ASN GLN PHE LEU          
SEQRES  12 D  260  THR GLN TYR PHE LEU HIS GLN GLN PRO ALA ASN CYS LYS          
SEQRES  13 D  260  VAL GLU SER LEU ALA MET PHE LEU GLY GLU LEU SER LEU          
SEQRES  14 D  260  ILE ASP ALA ASP PRO TYR LEU LYS TYR LEU PRO SER VAL          
SEQRES  15 D  260  ILE ALA GLY ALA ALA PHE HIS LEU ALA LEU TYR THR VAL          
SEQRES  16 D  260  THR GLY GLN SER TRP PRO GLU SER LEU ILE ARG LYS THR          
SEQRES  17 D  260  GLY TYR THR LEU GLU SER LEU LYS PRO CYS LEU MET ASP          
SEQRES  18 D  260  LEU HIS GLN THR TYR LEU LYS ALA PRO GLN HIS ALA GLN          
SEQRES  19 D  260  GLN SER ILE ARG GLU LYS TYR LYS ASN SER LYS TYR HIS          
SEQRES  20 D  260  GLY VAL SER LEU LEU ASN PRO PRO GLU THR LEU ASN LEU          
HET    BLZ  A 301      31                                                       
HET    BLZ  C 401      31                                                       
HETNAM     BLZ 5-[5,6-BIS(METHYLOXY)-1H-BENZIMIDAZOL-1-YL]-3-{[1-(2-            
HETNAM   2 BLZ  CHLOROPHENYL)ETHYL]OXY}-2-THIOPHENECARBOXAMIDE                  
FORMUL   5  BLZ    2(C22 H20 CL N3 O4 S)                                        
FORMUL   7  HOH   *242(H2 O)                                                    
HELIX    1   1 PRO A   45  LEU A   58  1                                  14    
HELIX    2   2 LEU A   87  SER A   94  1                                   8    
HELIX    3   3 PRO A  100  HIS A  121  1                                  22    
HELIX    4   4 LYS A  129  GLN A  131  5                                   3    
HELIX    5   5 ASP A  145  ALA A  149  5                                   5    
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  252  1                                   6    
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 TYR B  178  CYS B  193  1                                  16    
HELIX   16  16 TYR B  199  GLN B  203  5                                   5    
HELIX   17  17 THR B  207  TYR B  225  1                                  19    
HELIX   18  18 GLN B  228  SER B  244  1                                  17    
HELIX   19  19 LEU B  249  GLU B  269  1                                  21    
HELIX   20  20 GLU B  274  ILE B  281  1                                   8    
HELIX   21  21 THR B  287  LEU B  302  1                                  16    
HELIX   22  22 THR B  310  LEU B  320  1                                  11    
HELIX   23  23 ASN B  326  ASP B  343  1                                  18    
HELIX   24  24 ASP B  343  LEU B  348  1                                   6    
HELIX   25  25 LEU B  351  GLY B  369  1                                  19    
HELIX   26  26 PRO B  373  GLY B  381  1                                   9    
HELIX   27  27 THR B  383  ALA B  401  1                                  19    
HELIX   28  28 PRO B  402  HIS B  404  5                                   3    
HELIX   29  29 GLN B  407  TYR B  413  1                                   7    
HELIX   30  30 LYS B  414  HIS B  419  5                                   6    
HELIX   31  31 GLY B  420  LEU B  424  5                                   5    
HELIX   32  32 PRO C   45  LYS C   56  1                                  12    
HELIX   33  33 LEU C   87  SER C   94  1                                   8    
HELIX   34  34 PRO C  100  HIS C  121  1                                  22    
HELIX   35  35 THR C  165  ARG C  169  5                                   5    
HELIX   36  36 ALA C  170  LEU C  175  1                                   6    
HELIX   37  37 THR C  182  ARG C  199  1                                  18    
HELIX   38  38 SER C  207  GLY C  220  1                                  14    
HELIX   39  39 GLY C  229  MET C  233  5                                   5    
HELIX   40  40 ASP C  247  VAL C  252  1                                   6    
HELIX   41  41 ASP C  256  LEU C  267  1                                  12    
HELIX   42  42 SER C  276  LEU C  281  1                                   6    
HELIX   43  43 ALA C  282  GLN C  287  5                                   6    
HELIX   44  44 TYR D  178  CYS D  193  1                                  16    
HELIX   45  45 TYR D  199  GLN D  203  5                                   5    
HELIX   46  46 THR D  207  TYR D  225  1                                  19    
HELIX   47  47 GLN D  228  SER D  244  1                                  17    
HELIX   48  48 LEU D  249  GLY D  251  5                                   3    
HELIX   49  49 LYS D  252  GLU D  269  1                                  18    
HELIX   50  50 GLU D  274  ILE D  281  1                                   8    
HELIX   51  51 THR D  287  LEU D  302  1                                  16    
HELIX   52  52 THR D  310  LEU D  320  1                                  11    
HELIX   53  53 ASN D  326  ASP D  343  1                                  18    
HELIX   54  54 ASP D  343  LEU D  348  1                                   6    
HELIX   55  55 LEU D  351  THR D  368  1                                  18    
HELIX   56  56 PRO D  373  GLY D  381  1                                   9    
HELIX   57  57 THR D  383  ALA D  401  1                                  19    
HELIX   58  58 PRO D  402  HIS D  404  5                                   3    
HELIX   59  59 GLN D  407  TYR D  413  1                                   7    
HELIX   60  60 LYS D  414  HIS D  419  5                                   6    
HELIX   61  61 GLY D  420  LEU D  424  5                                   5    
SHEET    1   A 5 PHE A   4  GLY A  13  0                                        
SHEET    2   A 5 GLY A  16  ASN A  23 -1  O  VAL A  18   N  GLY A  11           
SHEET    3   A 5 VAL A  29  ILE A  35 -1  O  LEU A  32   N  TYR A  19           
SHEET    4   A 5 LEU A  76  GLU A  81 -1  O  LEU A  78   N  LYS A  33           
SHEET    5   A 5 LEU A  66  HIS A  71 -1  N  ILE A  70   O  TYR A  77           
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  GLY C  13  0                                        
SHEET    2   D 5 GLY C  16  ASN C  23 -1  O  LYS C  20   N  GLU C   8           
SHEET    3   D 5 VAL C  29  ILE C  35 -1  O  VAL C  30   N  ALA C  21           
SHEET    4   D 5 LEU C  76  GLU C  81 -1  O  LEU C  78   N  LYS C  33           
SHEET    5   D 5 LEU C  66  HIS C  71 -1  N  ASP C  68   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           
CISPEP   1 GLN B  323    PRO B  324          0       -11.80                     
CISPEP   2 ASP B  345    PRO B  346          0         9.67                     
CISPEP   3 GLN D  323    PRO D  324          0        -8.94                     
CISPEP   4 ASP D  345    PRO D  346          0         8.29                     
SITE     1 AC1 16 ILE A  10  TYR A  15  VAL A  18  ALA A  31                    
SITE     2 AC1 16 GLU A  51  PHE A  80  GLU A  81  PHE A  82                    
SITE     3 AC1 16 LEU A  83  HIS A  84  GLN A 131  ASN A 132                    
SITE     4 AC1 16 LEU A 134  ALA A 144  ASP A 145  HOH A 376                    
SITE     1 AC2 16 ILE C  10  TYR C  15  ALA C  31  LYS C  33                    
SITE     2 AC2 16 GLU C  51  VAL C  64  PHE C  80  GLU C  81                    
SITE     3 AC2 16 PHE C  82  LEU C  83  HIS C  84  GLN C 131                    
SITE     4 AC2 16 ASN C 132  LEU C 134  ALA C 144  ASP C 145                    
CRYST1  184.882  184.882  213.000  90.00  90.00 120.00 P 62 2 2     24          
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      0.005409  0.003123  0.000000        0.00000                         
SCALE2      0.000000  0.006246  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004695        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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