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Database: PDB
Entry: 4AZF
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HEADER    TRANSFERASE                             25-JUN-12   4AZF              
TITLE     HUMAN DYRK2 IN COMPLEX WITH LEUCETTINE L41                            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DYRK2 DUAL-SPECIFICITY TYROSINE-PHOSPHORYLATION REGULATED  
COMPND   3  KINASE 2;                                                           
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: DYRK2;                                                      
COMPND   6 EC: 2.7.11.1;                                                        
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.ELKINS,M.SOUNDARARAJAN,J.R.C.MUNIZ,T.TAHTOUH,G.BURGY,E.DURIEU,    
AUTHOR   2 O.LOZACH,C.COCHET,R.S.SCHMID,D.C.LO,F.DELHOMMEL,F.CARREAUX,          
AUTHOR   3 J.P.BAZUREAU,L.MEIJER,A.EDWARDS,C.BOUNTRA,S.KNAPP                    
REVDAT   3   21-NOV-12 4AZF    1       JRNL                                     
REVDAT   2   03-OCT-12 4AZF    1       JRNL   REMARK                            
REVDAT   1   05-SEP-12 4AZF    0                                                
JRNL        AUTH   T.TAHTOUH,J.M.ELKINS,P.FILIPPAKOPOULOS,M.SOUNDARARAJAN,      
JRNL        AUTH 2 G.BURGY,E.DURIEU,C.COCHET,R.S.SCHMID,D.C.LO,F.DELHOMMEL,     
JRNL        AUTH 3 A.OBERHOLZER,P.LAURENCE,F.CARREAUX,J.P.BAZUREAU,S.KNAPP,     
JRNL        AUTH 4 L.MEIJER                                                     
JRNL        TITL   SELECTIVITY, CO-CRYSTAL STRUCTURES AND NEUROPROTECTIVE       
JRNL        TITL 2 PROPERTIES OF LEUCETTINES, A FAMILY OF PROTEIN KINASE        
JRNL        TITL 3 INHIBITORS DERIVED FROM THE MARINE SPONGE ALKALOID           
JRNL        TITL 4 LEUCETTAMINE B.                                              
JRNL        REF    J.MED.CHEM.                   V.  55  9312 2012              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   22998443                                                     
JRNL        DOI    10.1021/JM301034U                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 74.27                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.88                          
REMARK   3   NUMBER OF REFLECTIONS             : 16896                          
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) : 0.19973                         
REMARK   3   R VALUE            (WORKING SET) : 0.19681                         
REMARK   3   FREE R VALUE                     : 0.25515                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.1                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 907                             
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) : 2.550                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.616                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1081                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.91                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.282                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 61                           
REMARK   3   BIN FREE R VALUE                    : 0.336                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3192                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 68                                      
REMARK   3   SOLVENT ATOMS            : 57                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.655                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.34                                                 
REMARK   3    B22 (A**2) : 1.34                                                 
REMARK   3    B33 (A**2) : -2.68                                                
REMARK   3    B12 (A**2) : 0.00                                                 
REMARK   3    B13 (A**2) : 0.00                                                 
REMARK   3    B23 (A**2) : 0.00                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.489         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.293         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.224         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 20.845        
REMARK   3                                                                      
REMARK   3  CORRELATION COEFFICIENTS.                                           
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.946                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.914                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  3340 ; 0.008 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  2271 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  4521 ; 1.378 ; 1.973       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5499 ; 0.859 ; 3.001       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   407 ; 5.871 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   155 ;34.858 ;23.677       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   555 ;15.100 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    21 ;19.054 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   475 ; 0.069 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3716 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   691 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
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    51        A    91                          
REMARK   3    ORIGIN FOR THE GROUP (A):  57.6470  26.5020  37.2490              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1348 T22:   0.3079                                     
REMARK   3      T33:   0.1385 T12:   0.0370                                     
REMARK   3      T13:  -0.0584 T23:   0.0812                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6748 L22:   2.3154                                     
REMARK   3      L33:   7.8647 L12:  -0.3258                                     
REMARK   3      L13:   0.9335 L23:   0.0739                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1146 S12:  -0.5130 S13:  -0.3779                       
REMARK   3      S21:   0.2509 S22:  -0.0939 S23:   0.0599                       
REMARK   3      S31:   0.1313 S32:   0.0227 S33:   0.2085                       
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):  45.2020  27.5930  21.2830              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1790 T22:   0.0158                                     
REMARK   3      T33:   0.0622 T12:   0.0201                                     
REMARK   3      T13:  -0.0974 T23:  -0.0174                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.2244 L22:   0.6934                                     
REMARK   3      L33:   1.9089 L12:   0.3175                                     
REMARK   3      L13:  -0.6272 L23:  -0.0210                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0807 S12:   0.2894 S13:  -0.1969                       
REMARK   3      S21:  -0.2992 S22:  -0.0259 S23:   0.1538                       
REMARK   3      S31:  -0.0457 S32:   0.0397 S33:   0.1066                       
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   467                          
REMARK   3    ORIGIN FOR THE GROUP (A):  12.9770  28.7010  11.9210              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0238 T22:   0.1262                                     
REMARK   3      T33:   0.0661 T12:   0.0400                                     
REMARK   3      T13:  -0.0080 T23:  -0.0411                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4238 L22:   1.5497                                     
REMARK   3      L33:   3.6536 L12:  -0.2457                                     
REMARK   3      L13:   0.8683 L23:  -0.2906                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1379 S12:  -0.1020 S13:   0.2362                       
REMARK   3      S21:   0.0531 S22:  -0.0896 S23:   0.1982                       
REMARK   3      S31:  -0.1315 S32:  -0.4850 S33:   0.2275                       
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          
REMARK   3   RIDING POSITIONS.                                                  
REMARK   4                                                                      
REMARK   4 4AZF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-JUN-12.                  
REMARK 100 THE PDBE ID CODE IS EBI-53047.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-SEP-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17843                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.55                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 59.02                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.9                                
REMARK 200  R MERGE                    (I) : 0.12                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.00                              
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.1                                
REMARK 200  R MERGE FOR SHELL          (I) : 0.88                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.50                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC5                                               
REMARK 200 STARTING MODEL: PDB ENTRY 3K2L                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.4                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.7                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M NA/KPO4, 20% PEG 3350, 10%         
REMARK 280  ETHYLENE GLYCOL                                                     
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       41.73050            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       41.73050            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       74.26700            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       41.73050            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       41.73050            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       74.26700            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       41.73050            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       41.73050            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       74.26700            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       41.73050            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       41.73050            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       74.26700            
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 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 A2007   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 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     HIS A  55    CG   ND1  CD2  CE1  NE2                             
REMARK 470     MET A  73    CG   SD   CE                                        
REMARK 470     LYS A  75    CE   NZ                                             
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 116    CD   CE   NZ                                        
REMARK 470     GLN A 134    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 157    CG   CD   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 241    NZ                                                  
REMARK 470     LYS A 268    NZ                                                  
REMARK 470     GLN A 286    CD   OE1  NE2                                       
REMARK 470     ARG A 305    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 371    NZ                                                  
REMARK 470     LYS A 377    CE   NZ                                             
REMARK 470     LYS A 380    NZ                                                  
REMARK 470     LYS A 386    CE   NZ                                             
REMARK 470     SER A 398    OG                                                  
REMARK 470     ASP A 431    CG   OD1  OD2                                       
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    THR A 122      105.79    -53.39                                   
REMARK 500    TYR A 147       27.17     48.85                                   
REMARK 500    LEU A 152      -53.87   -124.13                                   
REMARK 500    LEU A 231     -167.74   -118.27                                   
REMARK 500    SER A 232     -149.38   -105.49                                   
REMARK 500    PHE A 244       26.99     49.78                                   
REMARK 500    CYS A 274       -7.32     80.40                                   
REMARK 500    ASP A 275       48.97   -146.66                                   
REMARK 500    ASP A 295       77.52     61.33                                   
REMARK 500    PHE A 296       30.44    -93.54                                   
REMARK 500    PTR A 309      103.77    -57.06                                   
REMARK 500    GLN A 311      158.03     70.03                                   
REMARK 500    ALA A 375       42.68    -92.95                                   
REMARK 500    LYS A 428       53.26     37.72                                   
REMARK 500    ASP A 431       43.44   -105.99                                   
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 3RA A 600                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A1464                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A1465                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4AZE   RELATED DB: PDB                                   
REMARK 900  HUMAN DYRK1A IN COMPLEX WITH LEUCETTINE L41                         
DBREF  4AZF A   73   467  UNP    Q92630   DYRK2_HUMAN     73    467             
SEQADV 4AZF MET A   51  UNP  Q92630              EXPRESSION TAG                 
SEQADV 4AZF HIS A   52  UNP  Q92630              EXPRESSION TAG                 
SEQADV 4AZF HIS A   53  UNP  Q92630              EXPRESSION TAG                 
SEQADV 4AZF HIS A   54  UNP  Q92630              EXPRESSION TAG                 
SEQADV 4AZF HIS A   55  UNP  Q92630              EXPRESSION TAG                 
SEQADV 4AZF HIS A   56  UNP  Q92630              EXPRESSION TAG                 
SEQADV 4AZF HIS A   57  UNP  Q92630              EXPRESSION TAG                 
SEQADV 4AZF SER A   58  UNP  Q92630              EXPRESSION TAG                 
SEQADV 4AZF SEP A   59  UNP  Q92630              EXPRESSION TAG                 
SEQADV 4AZF GLY A   60  UNP  Q92630              EXPRESSION TAG                 
SEQADV 4AZF VAL A   61  UNP  Q92630              EXPRESSION TAG                 
SEQADV 4AZF ASP A   62  UNP  Q92630              EXPRESSION TAG                 
SEQADV 4AZF LEU A   63  UNP  Q92630              EXPRESSION TAG                 
SEQADV 4AZF GLY A   64  UNP  Q92630              EXPRESSION TAG                 
SEQADV 4AZF THR A   65  UNP  Q92630              EXPRESSION TAG                 
SEQADV 4AZF GLU A   66  UNP  Q92630              EXPRESSION TAG                 
SEQADV 4AZF ASN A   67  UNP  Q92630              EXPRESSION TAG                 
SEQADV 4AZF LEU A   68  UNP  Q92630              EXPRESSION TAG                 
SEQADV 4AZF TYR A   69  UNP  Q92630              EXPRESSION TAG                 
SEQADV 4AZF PHE A   70  UNP  Q92630              EXPRESSION TAG                 
SEQADV 4AZF GLN A   71  UNP  Q92630              EXPRESSION TAG                 
SEQADV 4AZF SER A   72  UNP  Q92630              EXPRESSION TAG                 
SEQRES   1 A  417  MET HIS HIS HIS HIS HIS HIS SER SEP GLY VAL ASP LEU          
SEQRES   2 A  417  GLY THR GLU ASN LEU TYR PHE GLN SER MET GLY LYS VAL          
SEQRES   3 A  417  LYS ALA THR PRO MET THR PRO GLU GLN ALA MET LYS GLN          
SEQRES   4 A  417  TYR MET GLN LYS LEU THR ALA PHE GLU HIS HIS GLU ILE          
SEQRES   5 A  417  PHE SER TYR PRO GLU ILE TYR PHE LEU GLY LEU ASN ALA          
SEQRES   6 A  417  LYS LYS ARG GLN GLY MET THR GLY GLY PRO ASN ASN GLY          
SEQRES   7 A  417  GLY TYR ASP ASP ASP GLN GLY SER TYR VAL GLN VAL PRO          
SEQRES   8 A  417  HIS ASP HIS VAL ALA TYR ARG TYR GLU VAL LEU LYS VAL          
SEQRES   9 A  417  ILE GLY LYS GLY SER PHE GLY GLN VAL VAL LYS ALA TYR          
SEQRES  10 A  417  ASP HIS LYS VAL HIS GLN HIS VAL ALA LEU LYS MET VAL          
SEQRES  11 A  417  ARG ASN GLU LYS ARG PHE HIS ARG GLN ALA ALA GLU GLU          
SEQRES  12 A  417  ILE ARG ILE LEU GLU HIS LEU ARG LYS GLN ASP LYS ASP          
SEQRES  13 A  417  ASN THR MET ASN VAL ILE HIS MET LEU GLU ASN PHE THR          
SEQRES  14 A  417  PHE ARG ASN HIS ILE CYS MET THR PHE GLU LEU LEU SER          
SEQRES  15 A  417  MET ASN LEU TYR GLU LEU ILE LYS LYS ASN LYS PHE GLN          
SEQRES  16 A  417  GLY PHE SER LEU PRO LEU VAL ARG LYS PHE ALA HIS SER          
SEQRES  17 A  417  ILE LEU GLN CYS LEU ASP ALA LEU HIS LYS ASN ARG ILE          
SEQRES  18 A  417  ILE HIS CYS ASP LEU LYS PRO GLU ASN ILE LEU LEU LYS          
SEQRES  19 A  417  GLN GLN GLY ARG SER GLY ILE LYS VAL ILE ASP PHE GLY          
SEQRES  20 A  417  SER SER CYS TYR GLU HIS GLN ARG VAL TYR THR PTR ILE          
SEQRES  21 A  417  GLN SER ARG PHE TYR ARG ALA PRO GLU VAL ILE LEU GLY          
SEQRES  22 A  417  ALA ARG TYR GLY MET PRO ILE ASP MET TRP SER LEU GLY          
SEQRES  23 A  417  CYS ILE LEU ALA GLU LEU LEU THR GLY TYR PRO LEU LEU          
SEQRES  24 A  417  PRO GLY GLU ASP GLU GLY ASP GLN LEU ALA CYS MET ILE          
SEQRES  25 A  417  GLU LEU LEU GLY MET PRO SER GLN LYS LEU LEU ASP ALA          
SEQRES  26 A  417  SER LYS ARG ALA LYS ASN PHE VAL SER SEP LYS GLY TYR          
SEQRES  27 A  417  PRO ARG TYR CYS THR VAL THR THR LEU SER ASP GLY SER          
SEQRES  28 A  417  VAL VAL LEU ASN GLY GLY ARG SER ARG ARG GLY LYS LEU          
SEQRES  29 A  417  ARG GLY PRO PRO GLU SER ARG GLU TRP GLY ASN ALA LEU          
SEQRES  30 A  417  LYS GLY CYS ASP ASP PRO LEU PHE LEU ASP PHE LEU LYS          
SEQRES  31 A  417  GLN CYS LEU GLU TRP ASP PRO ALA VAL ARG MET THR PRO          
SEQRES  32 A  417  GLY GLN ALA LEU ARG HIS PRO TRP LEU ARG ARG ARG LEU          
SEQRES  33 A  417  PRO                                                          
MODRES 4AZF SEP A   59  SER  PHOSPHOSERINE                                      
MODRES 4AZF PTR A  309  TYR  O-PHOSPHOTYROSINE                                  
MODRES 4AZF SEP A  385  SER  PHOSPHOSERINE                                      
HET    SEP  A  59      10                                                       
HET    PTR  A 309      16                                                       
HET    SEP  A 385      10                                                       
HET    3RA  A 600      23                                                       
HET    EDO  A1464       4                                                       
HET    PO4  A1465       5                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     3RA 5-(1,3-BENZODIOXOL-5-YLMETHYL)-2-                                
HETNAM   2 3RA  (PHENYLAMINO)-4H-IMIDAZOL-4-ONE                                 
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     PO4 PHOSPHATE ION                                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
HETSYN     PTR PHOSPHONOTYROSINE                                                
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   2  SEP    2(C3 H8 N O6 P)                                              
FORMUL   3  PTR    C9 H12 N O6 P                                                
FORMUL   4  3RA    C17 H13 N3 O3                                                
FORMUL   5  EDO    C2 H6 O2                                                     
FORMUL   6  PO4    O4 P 3-                                                      
FORMUL   7  HOH   *57(H2 O)                                                     
HELIX    1   1 ASP A   62  GLU A   66  5                                   5    
HELIX    2   2 THR A   82  MET A   91  1                                  10    
HELIX    3   3 GLN A   92  LEU A   94  5                                   3    
HELIX    4   4 THR A   95  ILE A  102  1                                   8    
HELIX    5   5 PHE A  103  TYR A  105  5                                   3    
HELIX    6   6 GLY A  124  GLY A  129  1                                   6    
HELIX    7   7 GLU A  183  LYS A  202  1                                  20    
HELIX    8   8 ASN A  234  ASN A  242  1                                   9    
HELIX    9   9 SER A  248  ASN A  269  1                                  22    
HELIX   10  10 LYS A  277  GLU A  279  5                                   3    
HELIX   11  11 SER A  312  ARG A  316  5                                   5    
HELIX   12  12 ALA A  317  GLY A  323  1                                   7    
HELIX   13  13 MET A  328  GLY A  345  1                                  18    
HELIX   14  14 ASP A  353  GLY A  366  1                                  14    
HELIX   15  15 SER A  369  ALA A  375  1                                   7    
HELIX   16  16 ARG A  378  VAL A  383  1                                   6    
HELIX   17  17 GLU A  422  LEU A  427  1                                   6    
HELIX   18  18 ASP A  432  LEU A  443  1                                  12    
HELIX   19  19 THR A  452  ARG A  458  1                                   7    
SHEET    1  AA 2 ASN A  67  TYR A  69  0                                        
SHEET    2  AA 2 LYS A  77  THR A  79 -1  O  LYS A  77   N  TYR A  69           
SHEET    1  AB 6 HIS A 144  VAL A 145  0                                        
SHEET    2  AB 6 TYR A 149  LYS A 157 -1  O  TYR A 149   N  VAL A 145           
SHEET    3  AB 6 GLY A 161  ASP A 168 -1  O  VAL A 163   N  ILE A 155           
SHEET    4  AB 6 GLN A 173  VAL A 180 -1  O  GLN A 173   N  ASP A 168           
SHEET    5  AB 6 HIS A 223  GLU A 229 -1  O  ILE A 224   N  VAL A 180           
SHEET    6  AB 6 MET A 214  PHE A 220 -1  N  LEU A 215   O  THR A 227           
SHEET    1  AC 2 ILE A 271  ILE A 272  0                                        
SHEET    2  AC 2 CYS A 300  TYR A 301 -1  O  CYS A 300   N  ILE A 272           
SHEET    1  AD 2 ILE A 281  LEU A 283  0                                        
SHEET    2  AD 2 ILE A 291  VAL A 293 -1  O  LYS A 292   N  LEU A 282           
SHEET    1  AE 2 VAL A 394  THR A 395  0                                        
SHEET    2  AE 2 VAL A 403  LEU A 404 -1  O  VAL A 403   N  THR A 395           
SHEET    1  AF 2 GLY A 407  ARG A 408  0                                        
SHEET    2  AF 2 LEU A 414  ARG A 415 -1  O  ARG A 415   N  GLY A 407           
LINK         N   SEP A  59                 C   SER A  58     1555   1555  1.34  
LINK         C   SEP A  59                 N   GLY A  60     1555   1555  1.33  
LINK         C   PTR A 309                 N   ILE A 310     1555   1555  1.33  
LINK         N   PTR A 309                 C   THR A 308     1555   1555  1.33  
LINK         C   SEP A 385                 N   LYS A 386     1555   1555  1.33  
LINK         N   SEP A 385                 C   SER A 384     1555   1555  1.32  
CISPEP   1 GLY A  123    GLY A  124          0         5.07                     
CISPEP   2 SER A  398    ASP A  399          0        -6.83                     
SITE     1 AC1 14 ILE A 155  GLY A 156  PHE A 160  VAL A 163                    
SITE     2 AC1 14 ALA A 176  LYS A 178  GLU A 229  LEU A 230                    
SITE     3 AC1 14 LEU A 231  LEU A 282  ILE A 294  ASP A 295                    
SITE     4 AC1 14 HOH A2028  HOH A2031                                          
SITE     1 AC2  1 ARG A 411                                                     
SITE     1 AC3  3 HIS A  56  HIS A  57  HIS A 174                               
CRYST1   83.461   83.461  148.534  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      0.011982  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011982  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006732        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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