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Database: PDB
Entry: 6HDR
LinkDB: 6HDR
Original site: 6HDR 
HEADER    TRANSFERASE                             18-AUG-18   6HDR              
TITLE     HUMAN DYRK2 BOUND TO CURCUMIN                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DUAL SPECIFICITY TYROSINE-PHOSPHORYLATION-REGULATED KINASE 
COMPND   3 2;                                                                   
COMPND   4 CHAIN: A;                                                            
COMPND   5 EC: 2.7.12.1;                                                        
COMPND   6 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: DYRK2;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: BL21(DE3)                               
KEYWDS    KINASE, STRUCTURAL GENOMICS CONSORTIUM, SGC, TRANSFERASE              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.ELKINS,M.SOUNDARARAJAN,M.VOLLMAR,T.KROJER,C.BOUNTRA,A.M.EDWARDS,  
AUTHOR   2 C.ARROWSMITH,S.KNAPP                                                 
REVDAT   1   28-AUG-19 6HDR    0                                                
JRNL        AUTH   J.M.ELKINS,S.KNAPP                                           
JRNL        TITL   DYRK2 BOUND TO CURCUMIN                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0230                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.30                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 26114                          
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) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.243                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1411                            
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1863                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.34                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2850                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 102                          
REMARK   3   BIN FREE R VALUE                    : 0.3240                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3219                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 40                                      
REMARK   3   SOLVENT ATOMS            : 128                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 72.46                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.11000                                              
REMARK   3    B22 (A**2) : 1.11000                                              
REMARK   3    B33 (A**2) : -2.22000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.221         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.196         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.158         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 12.228        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.919                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3344 ; 0.008 ; 0.014       
REMARK   3   BOND LENGTHS OTHERS               (A):  2924 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4522 ; 1.272 ; 1.669       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  6842 ; 0.827 ; 1.643       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   405 ; 6.240 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   179 ;31.725 ;21.732       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   559 ;14.914 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;19.742 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   411 ; 0.060 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3760 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   632 ; 0.001 ; 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):  1626 ; 3.225 ; 5.444       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1625 ; 3.223 ; 5.443       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2029 ; 4.456 ; 8.164       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  2030 ; 4.455 ; 8.165       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1718 ; 3.845 ; 5.820       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1713 ; 3.821 ; 5.806       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2488 ; 5.586 ; 8.576       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3697 ; 7.220 ;63.457       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3683 ; 7.228 ;63.298       
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  : 3                                          
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    55        A    91                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.1400  26.1650  37.0560              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1455 T22:   0.4073                                     
REMARK   3      T33:   0.0803 T12:   0.0681                                     
REMARK   3      T13:  -0.0675 T23:   0.1017                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1727 L22:   1.0276                                     
REMARK   3      L33:   8.1570 L12:  -1.0549                                     
REMARK   3      L13:   1.2073 L23:  -0.4941                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1065 S12:  -0.7283 S13:  -0.2642                       
REMARK   3      S21:   0.0798 S22:   0.1031 S23:   0.0042                       
REMARK   3      S31:  -0.2189 S32:  -0.1878 S33:   0.0034                       
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 :   A    92        A   231                          
REMARK   3    ORIGIN FOR THE GROUP (A):  44.9790  27.5090  21.3540              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1843 T22:   0.1024                                     
REMARK   3      T33:   0.0244 T12:   0.0058                                     
REMARK   3      T13:  -0.0477 T23:   0.0240                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.4739 L22:   0.8391                                     
REMARK   3      L33:   1.4172 L12:   0.3838                                     
REMARK   3      L13:  -0.5308 L23:   0.1516                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0584 S12:   0.1236 S13:   0.0438                       
REMARK   3      S21:  -0.1700 S22:  -0.0260 S23:   0.0161                       
REMARK   3      S31:  -0.0279 S32:   0.0020 S33:   0.0844                       
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   232        A   463                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.9120  28.6300  11.8390              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0254 T22:   0.2126                                     
REMARK   3      T33:   0.0703 T12:   0.0427                                     
REMARK   3      T13:   0.0005 T23:  -0.0188                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6036 L22:   1.6367                                     
REMARK   3      L33:   3.3249 L12:  -0.5107                                     
REMARK   3      L13:   0.7412 L23:  -0.0655                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0579 S12:  -0.0348 S13:   0.2806                       
REMARK   3      S21:  -0.0063 S22:  -0.1225 S23:   0.1732                       
REMARK   3      S31:   0.0055 S32:  -0.5575 S33:   0.1804                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
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 6HDR COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-AUG-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200011533.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-FEB-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I03                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9762                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 27566                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.260                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 5.900                              
REMARK 200  R MERGE                    (I) : 0.07200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.83600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: 4AZF                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.15                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.63                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M SODIUM POTASSIUM PHOSPHATE, 20%     
REMARK 280  PEG 3350 AND 10% ETHYLENE GLYCOL, VAPOR DIFFUSION, SITTING DROP,    
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       41.82100            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       41.82100            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       74.45800            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       41.82100            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       41.82100            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       74.45800            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       41.82100            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       41.82100            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       74.45800            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       41.82100            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       41.82100            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       74.45800            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 570 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 19580 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 691  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 694  LIES ON A SPECIAL POSITION.                          
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     MET A    51                                                      
REMARK 465     HIS A    52                                                      
REMARK 465     HIS A    53                                                      
REMARK 465     HIS A    54                                                      
REMARK 465     GLY A   400                                                      
REMARK 465     SER A   401                                                      
REMARK 465     ARG A   464                                                      
REMARK 465     ARG A   465                                                      
REMARK 465     LEU A   466                                                      
REMARK 465     PRO A   467                                                      
REMARK 465     LYS A   468                                                      
REMARK 465     PRO A   469                                                      
REMARK 465     PRO A   470                                                      
REMARK 465     THR A   471                                                      
REMARK 465     GLY A   472                                                      
REMARK 465     GLU A   473                                                      
REMARK 465     LYS A   474                                                      
REMARK 465     THR A   475                                                      
REMARK 465     SER A   476                                                      
REMARK 465     VAL A   477                                                      
REMARK 465     LYS A   478                                                      
REMARK 465     ARG A   479                                                      
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     PHE A  70    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN A  71    CG   CD   OE1  NE2                                  
REMARK 470     SER A  72    OG                                                  
REMARK 470     MET A  73    CG   SD   CE                                        
REMARK 470     LYS A  77    CE   NZ                                             
REMARK 470     LYS A  88    CD   CE   NZ                                        
REMARK 470     LYS A  93    NZ                                                  
REMARK 470     LYS A 157    CE   NZ                                             
REMARK 470     LYS A 184    CG   CD   CE   NZ                                   
REMARK 470     ARG A 185    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 188    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 202    CD   CE   NZ                                        
REMARK 470     LYS A 205    CG   CD   CE   NZ                                   
REMARK 470     LYS A 243    CE   NZ                                             
REMARK 470     GLN A 286    CD   OE1  NE2                                       
REMARK 470     GLN A 304    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 305    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 306    CG1  CG2                                            
REMARK 470     ARG A 325    CD   NE   CZ   NH1  NH2                             
REMARK 470     LYS A 380    CG   CD   CE   NZ                                   
REMARK 470     SER A 398    OG                                                  
REMARK 470     VAL A 402    CG1  CG2                                            
REMARK 470     ARG A 463    CD   NE   CZ   NH1  NH2                             
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    ASP A  62       59.29   -154.44                                   
REMARK 500    ARG A 148      -43.94   -145.42                                   
REMARK 500    LEU A 231     -145.29   -115.98                                   
REMARK 500    SER A 232     -157.65   -131.25                                   
REMARK 500    ASP A 275       47.97   -156.11                                   
REMARK 500    ASP A 295       77.21     60.97                                   
REMARK 500    GLU A 302      -14.06    -49.15                                   
REMARK 500    GLN A 304       49.56   -103.58                                   
REMARK 500    VAL A 306      -66.37   -135.24                                   
REMARK 500    GLN A 311      153.88     70.73                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: PLANAR GROUPS                                              
REMARK 500                                                                      
REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL                 
REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE                    
REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN                    
REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS                        
REMARK 500 AN RMSD GREATER THAN THIS VALUE                                      
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        RMS     TYPE                                    
REMARK 500    ARG A 253         0.14    SIDE CHAIN                              
REMARK 500    ARG A 270         0.17    SIDE CHAIN                              
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 CC9 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DTD A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PO4 A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Ligand residues SEP A 59          
REMARK 800  through GLY A 60 bound to SER A 58                                  
DBREF  6HDR A   73   479  UNP    Q92630   DYRK2_HUMAN     73    479             
SEQADV 6HDR MET A   51  UNP  Q92630              INITIATING METHIONINE          
SEQADV 6HDR HIS A   52  UNP  Q92630              EXPRESSION TAG                 
SEQADV 6HDR HIS A   53  UNP  Q92630              EXPRESSION TAG                 
SEQADV 6HDR HIS A   54  UNP  Q92630              EXPRESSION TAG                 
SEQADV 6HDR HIS A   55  UNP  Q92630              EXPRESSION TAG                 
SEQADV 6HDR HIS A   56  UNP  Q92630              EXPRESSION TAG                 
SEQADV 6HDR HIS A   57  UNP  Q92630              EXPRESSION TAG                 
SEQADV 6HDR SER A   58  UNP  Q92630              EXPRESSION TAG                 
SEQADV 6HDR SEP A   59  UNP  Q92630              EXPRESSION TAG                 
SEQADV 6HDR GLY A   60  UNP  Q92630              EXPRESSION TAG                 
SEQADV 6HDR VAL A   61  UNP  Q92630              EXPRESSION TAG                 
SEQADV 6HDR ASP A   62  UNP  Q92630              EXPRESSION TAG                 
SEQADV 6HDR LEU A   63  UNP  Q92630              EXPRESSION TAG                 
SEQADV 6HDR GLY A   64  UNP  Q92630              EXPRESSION TAG                 
SEQADV 6HDR THR A   65  UNP  Q92630              EXPRESSION TAG                 
SEQADV 6HDR GLU A   66  UNP  Q92630              EXPRESSION TAG                 
SEQADV 6HDR ASN A   67  UNP  Q92630              EXPRESSION TAG                 
SEQADV 6HDR LEU A   68  UNP  Q92630              EXPRESSION TAG                 
SEQADV 6HDR TYR A   69  UNP  Q92630              EXPRESSION TAG                 
SEQADV 6HDR PHE A   70  UNP  Q92630              EXPRESSION TAG                 
SEQADV 6HDR GLN A   71  UNP  Q92630              EXPRESSION TAG                 
SEQADV 6HDR SER A   72  UNP  Q92630              EXPRESSION TAG                 
SEQRES   1 A  429  MET HIS HIS HIS HIS HIS HIS SER SEP GLY VAL ASP LEU          
SEQRES   2 A  429  GLY THR GLU ASN LEU TYR PHE GLN SER MET GLY LYS VAL          
SEQRES   3 A  429  LYS ALA THR PRO MET THR PRO GLU GLN ALA MET LYS GLN          
SEQRES   4 A  429  TYR MET GLN LYS LEU THR ALA PHE GLU HIS HIS GLU ILE          
SEQRES   5 A  429  PHE SER TYR PRO GLU ILE TYR PHE LEU GLY LEU ASN ALA          
SEQRES   6 A  429  LYS LYS ARG GLN GLY MET THR GLY GLY PRO ASN ASN GLY          
SEQRES   7 A  429  GLY TYR ASP ASP ASP GLN GLY SER TYR VAL GLN VAL PRO          
SEQRES   8 A  429  HIS ASP HIS VAL ALA TYR ARG TYR GLU VAL LEU LYS VAL          
SEQRES   9 A  429  ILE GLY LYS GLY SER PHE GLY GLN VAL VAL LYS ALA TYR          
SEQRES  10 A  429  ASP HIS LYS VAL HIS GLN HIS VAL ALA LEU LYS MET VAL          
SEQRES  11 A  429  ARG ASN GLU LYS ARG PHE HIS ARG GLN ALA ALA GLU GLU          
SEQRES  12 A  429  ILE ARG ILE LEU GLU HIS LEU ARG LYS GLN ASP LYS ASP          
SEQRES  13 A  429  ASN THR MET ASN VAL ILE HIS MET LEU GLU ASN PHE THR          
SEQRES  14 A  429  PHE ARG ASN HIS ILE CYS MET THR PHE GLU LEU LEU SER          
SEQRES  15 A  429  MET ASN LEU TYR GLU LEU ILE LYS LYS ASN LYS PHE GLN          
SEQRES  16 A  429  GLY PHE SER LEU PRO LEU VAL ARG LYS PHE ALA HIS SER          
SEQRES  17 A  429  ILE LEU GLN CYS LEU ASP ALA LEU HIS LYS ASN ARG ILE          
SEQRES  18 A  429  ILE HIS CYS ASP LEU LYS PRO GLU ASN ILE LEU LEU LYS          
SEQRES  19 A  429  GLN GLN GLY ARG SER GLY ILE LYS VAL ILE ASP PHE GLY          
SEQRES  20 A  429  SER SER CYS TYR GLU HIS GLN ARG VAL TYR THR PTR ILE          
SEQRES  21 A  429  GLN SER ARG PHE TYR ARG ALA PRO GLU VAL ILE LEU GLY          
SEQRES  22 A  429  ALA ARG TYR GLY MET PRO ILE ASP MET TRP SER LEU GLY          
SEQRES  23 A  429  CYS ILE LEU ALA GLU LEU LEU THR GLY TYR PRO LEU LEU          
SEQRES  24 A  429  PRO GLY GLU ASP GLU GLY ASP GLN LEU ALA CYS MET ILE          
SEQRES  25 A  429  GLU LEU LEU GLY MET PRO SER GLN LYS LEU LEU ASP ALA          
SEQRES  26 A  429  SER LYS ARG ALA LYS ASN PHE VAL SER SEP LYS GLY TYR          
SEQRES  27 A  429  PRO ARG TYR CYS THR VAL THR THR LEU SER ASP GLY SER          
SEQRES  28 A  429  VAL VAL LEU ASN GLY GLY ARG SER ARG ARG GLY LYS LEU          
SEQRES  29 A  429  ARG GLY PRO PRO GLU SER ARG GLU TRP GLY ASN ALA LEU          
SEQRES  30 A  429  LYS GLY CYS ASP ASP PRO LEU PHE LEU ASP PHE LEU LYS          
SEQRES  31 A  429  GLN CYS LEU GLU TRP ASP PRO ALA VAL ARG MET THR PRO          
SEQRES  32 A  429  GLY GLN ALA LEU ARG HIS PRO TRP LEU ARG ARG ARG LEU          
SEQRES  33 A  429  PRO LYS PRO PRO THR GLY GLU LYS THR SER VAL LYS ARG          
MODRES 6HDR PTR A  309  TYR  MODIFIED RESIDUE                                   
MODRES 6HDR SEP A  385  SER  MODIFIED RESIDUE                                   
HET    SEP  A  59      10                                                       
HET    PTR  A 309      16                                                       
HET    SEP  A 385      10                                                       
HET    CC9  A 501      27                                                       
HET    DTD  A 502       8                                                       
HET    PO4  A 503       5                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     CC9 CURCUMIN                                                         
HETNAM     DTD DITHIANE DIOL                                                    
HETNAM     PO4 PHOSPHATE ION                                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     PTR PHOSPHONOTYROSINE                                                
HETSYN     CC9 (1E,6E)-1,7-BIS(4-HYDROXY-3-METHOXYPHENYL)HEPTA-1,6-             
HETSYN   2 CC9  DIENE-3,5-DIONE                                                 
FORMUL   1  SEP    2(C3 H8 N O6 P)                                              
FORMUL   1  PTR    C9 H12 N O6 P                                                
FORMUL   2  CC9    C21 H20 O6                                                   
FORMUL   3  DTD    C4 H8 O2 S2                                                  
FORMUL   4  PO4    O4 P 3-                                                      
FORMUL   5  HOH   *128(H2 O)                                                    
HELIX    1 AA1 ASP A   62  GLU A   66  5                                   5    
HELIX    2 AA2 THR A   82  MET A   91  1                                  10    
HELIX    3 AA3 GLN A   92  LEU A   94  5                                   3    
HELIX    4 AA4 THR A   95  ILE A  102  1                                   8    
HELIX    5 AA5 PHE A  103  TYR A  105  5                                   3    
HELIX    6 AA6 GLY A  124  GLY A  129  1                                   6    
HELIX    7 AA7 LYS A  184  LYS A  202  1                                  19    
HELIX    8 AA8 ASN A  234  ASN A  242  1                                   9    
HELIX    9 AA9 SER A  248  ARG A  270  1                                  23    
HELIX   10 AB1 LYS A  277  GLU A  279  5                                   3    
HELIX   11 AB2 SER A  312  ARG A  316  5                                   5    
HELIX   12 AB3 ALA A  317  GLY A  323  1                                   7    
HELIX   13 AB4 MET A  328  GLY A  345  1                                  18    
HELIX   14 AB5 ASP A  353  GLY A  366  1                                  14    
HELIX   15 AB6 SER A  369  ALA A  375  1                                   7    
HELIX   16 AB7 ARG A  378  PHE A  382  5                                   5    
HELIX   17 AB8 GLU A  422  LEU A  427  1                                   6    
HELIX   18 AB9 ASP A  432  LEU A  443  1                                  12    
HELIX   19 AC1 THR A  452  ARG A  458  1                                   7    
SHEET    1 AA1 2 ASN A  67  TYR A  69  0                                        
SHEET    2 AA1 2 LYS A  77  THR A  79 -1  O  LYS A  77   N  TYR A  69           
SHEET    1 AA2 6 HIS A 144  VAL A 145  0                                        
SHEET    2 AA2 6 TYR A 149  GLY A 158 -1  O  TYR A 149   N  VAL A 145           
SHEET    3 AA2 6 GLY A 161  ASP A 168 -1  O  TYR A 167   N  GLU A 150           
SHEET    4 AA2 6 GLN A 173  VAL A 180 -1  O  LEU A 177   N  VAL A 164           
SHEET    5 AA2 6 HIS A 223  PHE A 228 -1  O  MET A 226   N  LYS A 178           
SHEET    6 AA2 6 MET A 214  PHE A 220 -1  N  PHE A 218   O  CYS A 225           
SHEET    1 AA3 2 ILE A 271  ILE A 272  0                                        
SHEET    2 AA3 2 CYS A 300  TYR A 301 -1  O  CYS A 300   N  ILE A 272           
SHEET    1 AA4 2 ILE A 281  LEU A 283  0                                        
SHEET    2 AA4 2 ILE A 291  VAL A 293 -1  O  LYS A 292   N  LEU A 282           
SHEET    1 AA5 2 VAL A 394  THR A 395  0                                        
SHEET    2 AA5 2 VAL A 403  LEU A 404 -1  O  VAL A 403   N  THR A 395           
SHEET    1 AA6 2 GLY A 407  ARG A 408  0                                        
SHEET    2 AA6 2 LEU A 414  ARG A 415 -1  O  ARG A 415   N  GLY A 407           
LINK         C   SER A  58                 N   SEP A  59     1555   1555  1.34  
LINK         C   SEP A  59                 N   GLY A  60     1555   1555  1.34  
LINK         C   THR A 308                 N   PTR A 309     1555   1555  1.34  
LINK         C   PTR A 309                 N   ILE A 310     1555   1555  1.34  
LINK         C   SER A 384                 N   SEP A 385     1555   1555  1.33  
LINK         C   SEP A 385                 N   LYS A 386     1555   1555  1.34  
SITE     1 AC1 14 LYS A 153  ILE A 155  PHE A 160  ALA A 176                    
SITE     2 AC1 14 LYS A 178  GLU A 193  ILE A 212  PHE A 228                    
SITE     3 AC1 14 GLU A 229  LEU A 230  LEU A 231  LEU A 282                    
SITE     4 AC1 14 ASP A 295  PHE A 296                                          
SITE     1 AC2  5 ILE A 155  ASN A 234  GLU A 279  HOH A 606                    
SITE     2 AC2  5 HOH A 619                                                     
SITE     1 AC3  4 HIS A  56  HIS A  57  HIS A 174  HOH A 631                    
SITE     1 AC4  5 HIS A  57  SER A  58  VAL A  61  TYR A 167                    
SITE     2 AC4  5 HIS A 172                                                     
CRYST1   83.642   83.642  148.916  90.00  90.00  90.00 P 42 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011956  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011956  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006715        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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