GenomeNet

Database: PDB
Entry: 5IF1
LinkDB: 5IF1
Original site: 5IF1 
HEADER    TRANSFERASE                             25-FEB-16   5IF1              
TITLE     CRYSTAL STRUCTURE APO CDK2/CYCLIN A                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYCLIN-DEPENDENT KINASE 2;                                 
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 SYNONYM: CELL DIVISION PROTEIN KINASE 2,P33 PROTEIN KINASE;          
COMPND   5 EC: 2.7.11.22;                                                       
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: CYCLIN-A2;                                                 
COMPND   9 CHAIN: B, D;                                                         
COMPND  10 SYNONYM: CYCLIN-A;                                                   
COMPND  11 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, CDKN2;                                                   
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: CCNA2, CCN1, CCNA;                                             
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    ANTINEOPLASTIC AGENTS, CYCLIN-DEPENDENT KINASES, DOSE-RESPONSE        
KEYWDS   2 RELATIONSHIP, DRUG, DRUG DISCOVERY, HELA CELLS, MOLECULAR STRUCTURE, 
KEYWDS   3 NEOPLASMS, PROTEIN KINASE INHIBITORS, PYRIMIDINES, STRUCTURE-        
KEYWDS   4 ACTIVITY RELATIONSHIP, STRUCTURE-KINETICS RELATIONSHIP, SULFOXIDES,  
KEYWDS   5 BIOPHYSICAL ASSAYS, TUMOR, HUMANS, TRANSFERASE                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.AYAZ,D.ANDRES,D.A.KWIATKOWSKI,C.KOLBE,P.LIENAU,G.SIEMEISTER,        
AUTHOR   2 U.LUECKING,C.M.STEGMANN                                              
REVDAT   4   21-AUG-19 5IF1    1       REMARK                                   
REVDAT   3   29-JUN-16 5IF1    1       JRNL                                     
REVDAT   2   04-MAY-16 5IF1    1       JRNL                                     
REVDAT   1   27-APR-16 5IF1    0                                                
JRNL        AUTH   P.AYAZ,D.ANDRES,D.A.KWIATKOWSKI,C.C.KOLBE,P.LIENAU,          
JRNL        AUTH 2 G.SIEMEISTER,U.LUCKING,C.M.STEGMANN                          
JRNL        TITL   CONFORMATIONAL ADAPTION MAY EXPLAIN THE SLOW DISSOCIATION    
JRNL        TITL 2 KINETICS OF RONICICLIB (BAY 1000394), A TYPE I CDK INHIBITOR 
JRNL        TITL 3 WITH KINETIC SELECTIVITY FOR CDK2 AND CDK9.                  
JRNL        REF    ACS CHEM.BIOL.                V.  11  1710 2016              
JRNL        REFN                   ESSN 1554-8937                               
JRNL        PMID   27090615                                                     
JRNL        DOI    10.1021/ACSCHEMBIO.6B00074                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.61 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.61                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.07                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 63451                          
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) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.187                           
REMARK   3   FREE R VALUE                     : 0.236                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3312                            
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) : 2.61                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.68                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4634                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.98                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3280                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 215                          
REMARK   3   BIN FREE R VALUE                    : 0.3600                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8918                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 121                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 60.55                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.60000                                              
REMARK   3    B22 (A**2) : 0.60000                                              
REMARK   3    B33 (A**2) : -1.96000                                             
REMARK   3    B12 (A**2) : 0.30000                                              
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): 0.287         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.237         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.189         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.271         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.930                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9165 ; 0.015 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  8950 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12444 ; 1.900 ; 1.975       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 20635 ; 1.089 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1110 ; 7.609 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   396 ;41.246 ;23.889       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1620 ;18.394 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;17.738 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1410 ; 0.106 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10093 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  2053 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  4434 ; 7.210 ; 3.802       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4433 ; 7.207 ; 3.801       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  5537 ; 9.913 ; 6.414       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  5538 ; 9.914 ; 6.415       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4731 ; 8.108 ; 4.198       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  4731 ; 8.107 ; 4.198       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  6904 ;11.429 ; 6.887       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 10232 ;13.667 ;25.485       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2): 10223 ;13.671 ;25.490       
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 : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
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 5IF1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-FEB-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000218700.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
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               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.918                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 63451                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.610                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.070                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM HEPES, 5MM DTT, 0.5 MM KCL,        
REMARK 280  875MM AMMONIUM SULFATE, PH 7.0, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  TEMPERATURE 277.15K                                                 
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      142.04667            
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       71.02333            
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      142.04667            
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       71.02333            
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      142.04667            
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       71.02333            
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      142.04667            
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       71.02333            
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: 3070 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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: 2970 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23470 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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     HIS B   168                                                      
REMARK 465     HIS B   169                                                      
REMARK 465     HIS B   170                                                      
REMARK 465     HIS B   171                                                      
REMARK 465     HIS B   172                                                      
REMARK 465     HIS B   173                                                      
REMARK 465     GLU B   174                                                      
REMARK 465     VAL B   175                                                      
REMARK 465     ARG C   297                                                      
REMARK 465     LEU C   298                                                      
REMARK 465     HIS D   168                                                      
REMARK 465     HIS D   169                                                      
REMARK 465     HIS D   170                                                      
REMARK 465     HIS D   171                                                      
REMARK 465     HIS D   172                                                      
REMARK 465     HIS D   173                                                      
REMARK 465     GLU D   174                                                      
REMARK 465     VAL D   175                                                      
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     THR A  39    OG1  CG2                                            
REMARK 470     GLU A  40    CG   CD   OE1  OE2                                  
REMARK 470     THR C  39    OG1  CG2                                            
REMARK 470     GLU C  40    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   343     O    HOH A   343    11455     0.83            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 214   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG A 217   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG B 241   NE  -  CZ  -  NH1 ANGL. DEV. =   3.6 DEGREES          
REMARK 500    ARG C  36   NE  -  CZ  -  NH1 ANGL. DEV. =   3.7 DEGREES          
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    THR A  14       45.42     33.98                                   
REMARK 500    TYR A  15      128.22     40.69                                   
REMARK 500    LEU A  37       63.46     61.67                                   
REMARK 500    ASP A  38     -109.21     28.67                                   
REMARK 500    THR A  39      -33.85    111.14                                   
REMARK 500    THR A  41     -168.47     43.97                                   
REMARK 500    ARG A 126      -16.40     75.85                                   
REMARK 500    ASP A 145       86.52     43.73                                   
REMARK 500    PRO A 155      140.34    -36.06                                   
REMARK 500    THR A 165      154.13    -46.95                                   
REMARK 500    CYS A 177      151.78    -45.01                                   
REMARK 500    GLN A 287      -56.29    -23.53                                   
REMARK 500    ARG B 250      -56.99     -2.19                                   
REMARK 500    PHE B 304       18.08     54.49                                   
REMARK 500    THR C  14      -80.24     22.19                                   
REMARK 500    GLU C  40       41.75   -143.61                                   
REMARK 500    THR C  41      -49.32   -162.22                                   
REMARK 500    GLU C  42      -50.71   -122.96                                   
REMARK 500    GLU C  73      -78.84    -12.48                                   
REMARK 500    HIS C 121       32.43    -93.71                                   
REMARK 500    ARG C 126       -3.93     80.62                                   
REMARK 500    ASP C 127       42.29   -150.24                                   
REMARK 500    ASP C 145       79.01     53.76                                   
REMARK 500    THR C 160       81.55     40.91                                   
REMARK 500    VAL C 163       40.53   -105.54                                   
REMARK 500    THR C 165     -167.37   -116.22                                   
REMARK 500    TRP C 227       82.24   -153.94                                   
REMARK 500    SER C 239      -34.40    -32.83                                   
REMARK 500    ASP C 256     -176.29    -66.73                                   
REMARK 500    ASP D 283       35.96     80.74                                   
REMARK 500    ASP D 284       48.35     34.73                                   
REMARK 500    PHE D 304       15.13     57.21                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU C   37     ASP C   38                   45.37                    
REMARK 500 THR C   72     GLU C   73                  147.42                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5IF1 A    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  5IF1 B  174   432  UNP    P20248   CCNA2_HUMAN    174    432             
DBREF  5IF1 C    1   298  UNP    P24941   CDK2_HUMAN       1    298             
DBREF  5IF1 D  174   432  UNP    P20248   CCNA2_HUMAN    174    432             
SEQADV 5IF1 HIS B  168  UNP  P20248              EXPRESSION TAG                 
SEQADV 5IF1 HIS B  169  UNP  P20248              EXPRESSION TAG                 
SEQADV 5IF1 HIS B  170  UNP  P20248              EXPRESSION TAG                 
SEQADV 5IF1 HIS B  171  UNP  P20248              EXPRESSION TAG                 
SEQADV 5IF1 HIS B  172  UNP  P20248              EXPRESSION TAG                 
SEQADV 5IF1 HIS B  173  UNP  P20248              EXPRESSION TAG                 
SEQADV 5IF1 HIS D  168  UNP  P20248              EXPRESSION TAG                 
SEQADV 5IF1 HIS D  169  UNP  P20248              EXPRESSION TAG                 
SEQADV 5IF1 HIS D  170  UNP  P20248              EXPRESSION TAG                 
SEQADV 5IF1 HIS D  171  UNP  P20248              EXPRESSION TAG                 
SEQADV 5IF1 HIS D  172  UNP  P20248              EXPRESSION TAG                 
SEQADV 5IF1 HIS D  173  UNP  P20248              EXPRESSION TAG                 
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  265  HIS HIS HIS HIS HIS HIS GLU VAL PRO ASP TYR HIS GLU          
SEQRES   2 B  265  ASP ILE HIS THR TYR LEU ARG GLU MET GLU VAL LYS CYS          
SEQRES   3 B  265  LYS PRO LYS VAL GLY TYR MET LYS LYS GLN PRO ASP ILE          
SEQRES   4 B  265  THR ASN SER MET ARG ALA ILE LEU VAL ASP TRP LEU VAL          
SEQRES   5 B  265  GLU VAL GLY GLU GLU TYR LYS LEU GLN ASN GLU THR LEU          
SEQRES   6 B  265  HIS LEU ALA VAL ASN TYR ILE ASP ARG PHE LEU SER SER          
SEQRES   7 B  265  MET SER VAL LEU ARG GLY LYS LEU GLN LEU VAL GLY THR          
SEQRES   8 B  265  ALA ALA MET LEU LEU ALA SER LYS PHE GLU GLU ILE TYR          
SEQRES   9 B  265  PRO PRO GLU VAL ALA GLU PHE VAL TYR ILE THR ASP ASP          
SEQRES  10 B  265  THR TYR THR LYS LYS GLN VAL LEU ARG MET GLU HIS LEU          
SEQRES  11 B  265  VAL LEU LYS VAL LEU THR PHE ASP LEU ALA ALA PRO THR          
SEQRES  12 B  265  VAL ASN GLN PHE LEU THR GLN TYR PHE LEU HIS GLN GLN          
SEQRES  13 B  265  PRO ALA ASN CYS LYS VAL GLU SER LEU ALA MET PHE LEU          
SEQRES  14 B  265  GLY GLU LEU SER LEU ILE ASP ALA ASP PRO TYR LEU LYS          
SEQRES  15 B  265  TYR LEU PRO SER VAL ILE ALA GLY ALA ALA PHE HIS LEU          
SEQRES  16 B  265  ALA LEU TYR THR VAL THR GLY GLN SER TRP PRO GLU SER          
SEQRES  17 B  265  LEU ILE ARG LYS THR GLY TYR THR LEU GLU SER LEU LYS          
SEQRES  18 B  265  PRO CYS LEU MET ASP LEU HIS GLN THR TYR LEU LYS ALA          
SEQRES  19 B  265  PRO GLN HIS ALA GLN GLN SER ILE ARG GLU LYS TYR LYS          
SEQRES  20 B  265  ASN SER LYS TYR HIS GLY VAL SER LEU LEU ASN PRO PRO          
SEQRES  21 B  265  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  265  HIS HIS HIS HIS HIS HIS GLU VAL PRO ASP TYR HIS GLU          
SEQRES   2 D  265  ASP ILE HIS THR TYR LEU ARG GLU MET GLU VAL LYS CYS          
SEQRES   3 D  265  LYS PRO LYS VAL GLY TYR MET LYS LYS GLN PRO ASP ILE          
SEQRES   4 D  265  THR ASN SER MET ARG ALA ILE LEU VAL ASP TRP LEU VAL          
SEQRES   5 D  265  GLU VAL GLY GLU GLU TYR LYS LEU GLN ASN GLU THR LEU          
SEQRES   6 D  265  HIS LEU ALA VAL ASN TYR ILE ASP ARG PHE LEU SER SER          
SEQRES   7 D  265  MET SER VAL LEU ARG GLY LYS LEU GLN LEU VAL GLY THR          
SEQRES   8 D  265  ALA ALA MET LEU LEU ALA SER LYS PHE GLU GLU ILE TYR          
SEQRES   9 D  265  PRO PRO GLU VAL ALA GLU PHE VAL TYR ILE THR ASP ASP          
SEQRES  10 D  265  THR TYR THR LYS LYS GLN VAL LEU ARG MET GLU HIS LEU          
SEQRES  11 D  265  VAL LEU LYS VAL LEU THR PHE ASP LEU ALA ALA PRO THR          
SEQRES  12 D  265  VAL ASN GLN PHE LEU THR GLN TYR PHE LEU HIS GLN GLN          
SEQRES  13 D  265  PRO ALA ASN CYS LYS VAL GLU SER LEU ALA MET PHE LEU          
SEQRES  14 D  265  GLY GLU LEU SER LEU ILE ASP ALA ASP PRO TYR LEU LYS          
SEQRES  15 D  265  TYR LEU PRO SER VAL ILE ALA GLY ALA ALA PHE HIS LEU          
SEQRES  16 D  265  ALA LEU TYR THR VAL THR GLY GLN SER TRP PRO GLU SER          
SEQRES  17 D  265  LEU ILE ARG LYS THR GLY TYR THR LEU GLU SER LEU LYS          
SEQRES  18 D  265  PRO CYS LEU MET ASP LEU HIS GLN THR TYR LEU LYS ALA          
SEQRES  19 D  265  PRO GLN HIS ALA GLN GLN SER ILE ARG GLU LYS TYR LYS          
SEQRES  20 D  265  ASN SER LYS TYR HIS GLY VAL SER LEU LEU ASN PRO PRO          
SEQRES  21 D  265  GLU THR LEU ASN LEU                                          
FORMUL   5  HOH   *121(H2 O)                                                    
HELIX    1 AA1 PRO A   45  LYS A   56  1                                  12    
HELIX    2 AA2 LEU A   87  SER A   94  1                                   8    
HELIX    3 AA3 PRO A  100  HIS A  121  1                                  22    
HELIX    4 AA4 LYS A  129  GLN A  131  5                                   3    
HELIX    5 AA5 THR A  165  ARG A  169  5                                   5    
HELIX    6 AA6 ALA A  170  LEU A  175  1                                   6    
HELIX    7 AA7 THR A  182  ARG A  199  1                                  18    
HELIX    8 AA8 SER A  207  GLY A  220  1                                  14    
HELIX    9 AA9 GLY A  229  MET A  233  5                                   5    
HELIX   10 AB1 ASP A  247  VAL A  252  1                                   6    
HELIX   11 AB2 ASP A  256  LEU A  267  1                                  12    
HELIX   12 AB3 SER A  276  ALA A  282  1                                   7    
HELIX   13 AB4 HIS A  283  GLN A  287  5                                   5    
HELIX   14 AB5 TYR B  178  CYS B  193  1                                  16    
HELIX   15 AB6 THR B  207  TYR B  225  1                                  19    
HELIX   16 AB7 GLN B  228  SER B  244  1                                  17    
HELIX   17 AB8 LYS B  252  GLU B  269  1                                  18    
HELIX   18 AB9 GLU B  274  ILE B  281  1                                   8    
HELIX   19 AC1 THR B  287  THR B  303  1                                  17    
HELIX   20 AC2 THR B  310  LEU B  320  1                                  11    
HELIX   21 AC3 ASN B  326  LEU B  341  1                                  16    
HELIX   22 AC4 ASP B  343  LEU B  348  1                                   6    
HELIX   23 AC5 LEU B  351  GLY B  369  1                                  19    
HELIX   24 AC6 PRO B  373  GLY B  381  1                                   9    
HELIX   25 AC7 THR B  383  ALA B  401  1                                  19    
HELIX   26 AC8 GLN B  407  TYR B  413  1                                   7    
HELIX   27 AC9 GLY B  420  LEU B  424  5                                   5    
HELIX   28 AD1 PRO C   45  LYS C   56  1                                  12    
HELIX   29 AD2 LEU C   87  SER C   94  1                                   8    
HELIX   30 AD3 PRO C  100  HIS C  121  1                                  22    
HELIX   31 AD4 LYS C  129  GLN C  131  5                                   3    
HELIX   32 AD5 ALA C  170  LEU C  175  1                                   6    
HELIX   33 AD6 THR C  182  THR C  198  1                                  17    
HELIX   34 AD7 SER C  207  GLY C  220  1                                  14    
HELIX   35 AD8 GLY C  229  MET C  233  5                                   5    
HELIX   36 AD9 ASP C  247  VAL C  252  1                                   6    
HELIX   37 AE1 ASP C  256  LEU C  267  1                                  12    
HELIX   38 AE2 SER C  276  ALA C  282  1                                   7    
HELIX   39 AE3 HIS C  283  GLN C  287  5                                   5    
HELIX   40 AE4 TYR D  178  CYS D  193  1                                  16    
HELIX   41 AE5 THR D  207  TYR D  225  1                                  19    
HELIX   42 AE6 GLN D  228  SER D  244  1                                  17    
HELIX   43 AE7 LEU D  249  GLY D  251  5                                   3    
HELIX   44 AE8 LYS D  252  GLU D  269  1                                  18    
HELIX   45 AE9 GLU D  274  THR D  282  1                                   9    
HELIX   46 AF1 THR D  287  LEU D  302  1                                  16    
HELIX   47 AF2 THR D  310  LEU D  320  1                                  11    
HELIX   48 AF3 ASN D  326  SER D  340  1                                  15    
HELIX   49 AF4 ASP D  343  LEU D  348  1                                   6    
HELIX   50 AF5 LEU D  351  THR D  368  1                                  18    
HELIX   51 AF6 PRO D  373  GLY D  381  1                                   9    
HELIX   52 AF7 THR D  383  ALA D  401  1                                  19    
HELIX   53 AF8 PRO D  402  HIS D  404  5                                   3    
HELIX   54 AF9 GLN D  407  LYS D  414  1                                   8    
HELIX   55 AG1 ASN D  415  HIS D  419  5                                   5    
HELIX   56 AG2 GLY D  420  LEU D  424  5                                   5    
SHEET    1 AA1 5 PHE A   4  GLU A  12  0                                        
SHEET    2 AA1 5 VAL A  17  ASN A  23 -1  O  LYS A  20   N  GLU A   8           
SHEET    3 AA1 5 VAL A  29  ILE A  35 -1  O  VAL A  30   N  ALA A  21           
SHEET    4 AA1 5 LEU A  76  GLU A  81 -1  O  PHE A  80   N  ALA A  31           
SHEET    5 AA1 5 LEU A  66  HIS A  71 -1  N  LEU A  67   O  VAL A  79           
SHEET    1 AA2 3 GLN A  85  ASP A  86  0                                        
SHEET    2 AA2 3 LEU A 133  ILE A 135 -1  O  ILE A 135   N  GLN A  85           
SHEET    3 AA2 3 ILE A 141  LEU A 143 -1  O  LYS A 142   N  LEU A 134           
SHEET    1 AA3 2 VAL A 123  LEU A 124  0                                        
SHEET    2 AA3 2 ARG A 150  ALA A 151 -1  O  ARG A 150   N  LEU A 124           
SHEET    1 AA4 5 PHE C   4  GLY C  11  0                                        
SHEET    2 AA4 5 VAL C  18  ASN C  23 -1  O  LYS C  20   N  GLU C   8           
SHEET    3 AA4 5 VAL C  29  ARG C  36 -1  O  VAL C  30   N  ALA C  21           
SHEET    4 AA4 5 LYS C  75  GLU C  81 -1  O  LEU C  78   N  LYS C  33           
SHEET    5 AA4 5 LEU C  66  HIS C  71 -1  N  LEU C  67   O  VAL C  79           
SHEET    1 AA5 3 GLN C  85  ASP C  86  0                                        
SHEET    2 AA5 3 LEU C 133  ILE C 135 -1  O  ILE C 135   N  GLN C  85           
SHEET    3 AA5 3 ILE C 141  LEU C 143 -1  O  LYS C 142   N  LEU C 134           
SHEET    1 AA6 2 VAL C 123  LEU C 124  0                                        
SHEET    2 AA6 2 ARG C 150  ALA C 151 -1  O  ARG C 150   N  LEU C 124           
CISPEP   1 TYR A   15    GLY A   16          0       -13.97                     
CISPEP   2 LEU A   37    ASP A   38          0        15.03                     
CISPEP   3 THR A   39    GLU A   40          0        -2.56                     
CISPEP   4 GLN B  323    PRO B  324          0       -14.10                     
CISPEP   5 ASP B  345    PRO B  346          0         6.75                     
CISPEP   6 TYR C   15    GLY C   16          0       -10.58                     
CISPEP   7 THR C  160    HIS C  161          0         0.10                     
CISPEP   8 HIS C  161    GLU C  162          0        20.31                     
CISPEP   9 VAL C  164    THR C  165          0        26.33                     
CISPEP  10 GLN D  323    PRO D  324          0       -15.52                     
CISPEP  11 ASP D  345    PRO D  346          0         8.82                     
CRYST1  186.574  186.574  213.070  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      0.005360  0.003094  0.000000        0.00000                         
SCALE2      0.000000  0.006189  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004693        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system