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Database: PDB
Entry: 5LXD
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HEADER    TRANSFERASE                             20-SEP-16   5LXD              
TITLE     CRYSTAL STRUCTURE OF DYRK2 IN COMPLEX WITH EHT 1610 (COMPOUND 2)      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DUAL SPECIFICITY TYROSINE-PHOSPHORYLATION-REGULATED KINASE 
COMPND   3 2;                                                                   
COMPND   4 CHAIN: A, B;                                                         
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: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VARIANT: R3-PRARE2;                                
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    TRANSFERASE, KINASE, INHIBITOR, UNUSUAL BINDING MODE, STRUCTURAL      
KEYWDS   2 GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.CHAIKUAD,F.VON DELFT,C.H.ARROWSMITH,A.EDWARDS,C.BOUNTRA,T.BESSON,   
AUTHOR   2 S.KNAPP,STRUCTURAL GENOMICS CONSORTIUM (SGC)                         
REVDAT   2   11-JAN-17 5LXD    1       JRNL                                     
REVDAT   1   26-OCT-16 5LXD    0                                                
JRNL        AUTH   A.CHAIKUAD,J.DIHARCE,M.SCHRODER,A.FOUCOURT,B.LEBLOND,        
JRNL        AUTH 2 A.S.CASAGRANDE,L.DESIRE,P.BONNET,S.KNAPP,T.BESSON            
JRNL        TITL   AN UNUSUAL BINDING MODEL OF THE METHYL                       
JRNL        TITL 2 9-ANILINOTHIAZOLO[5,4-F] QUINAZOLINE-2-CARBIMIDATES (EHT     
JRNL        TITL 3 1610 AND EHT 5372) CONFERS HIGH SELECTIVITY FOR              
JRNL        TITL 4 DUAL-SPECIFICITY TYROSINE PHOSPHORYLATION-REGULATED KINASES. 
JRNL        REF    J. MED. CHEM.                 V.  59 10315 2016              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   27766861                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.6B01083                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.58 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.58                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.04                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 33703                          
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) : 0.200                           
REMARK   3   R VALUE            (WORKING SET) : 0.197                           
REMARK   3   FREE R VALUE                     : 0.253                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1773                            
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) : 2.58                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.65                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2518                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.40                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3240                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 112                          
REMARK   3   BIN FREE R VALUE                    : 0.3980                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6223                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 94                                      
REMARK   3   SOLVENT ATOMS            : 193                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 44.60                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 66.99                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.64000                                             
REMARK   3    B22 (A**2) : -4.99000                                             
REMARK   3    B33 (A**2) : 6.63000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.51000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.486         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.295         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.255         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 23.618        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.920                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6503 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  6236 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8759 ; 1.179 ; 1.979       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 14333 ; 0.678 ; 3.002       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   782 ; 6.200 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   308 ;33.608 ;23.377       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1157 ;15.184 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    50 ;19.344 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   906 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  7300 ; 0.007 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1564 ; 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):  3098 ; 1.832 ; 3.401       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  3097 ; 1.832 ; 3.400       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3872 ; 2.987 ; 5.099       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3873 ; 2.987 ; 5.099       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3404 ; 2.029 ; 3.677       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  3404 ; 2.026 ; 3.677       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  4881 ; 3.322 ; 5.402       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  7512 ; 5.375 ;27.582       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  7513 ; 5.375 ;27.587       
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 : 4                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A     81       A     110      2                      
REMARK   3           1     B     81       B     110      2                      
REMARK   3           2     A    111       A     144      2                      
REMARK   3           2     B    111       B     144      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    594 ; 0.010 ; 0.500           
REMARK   3   TIGHT THERMAL      1    A (A**2):    373 ; 2.140 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    594 ; 2.370 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 2                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    145       A     390      2                      
REMARK   3           1     B    145       B     390      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  2    A    (A):   2601 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      2    A (A**2):   1457 ; 1.970 ; 0.500           
REMARK   3   MEDIUM THERMAL     2    A (A**2):   2601 ; 2.420 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 3                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    391       A     420      2                      
REMARK   3           1     B    391       B     420      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  3    A    (A):    263 ; 0.010 ; 0.500           
REMARK   3   TIGHT THERMAL      3    A (A**2):    173 ; 1.470 ; 0.500           
REMARK   3   MEDIUM THERMAL     3    A (A**2):    263 ; 1.450 ; 2.000           
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 4                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 1                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A    421       A     465      2                      
REMARK   3           1     B    421       B     465      2                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   MEDIUM POSITIONAL  4    A    (A):    464 ; 0.020 ; 0.500           
REMARK   3   TIGHT THERMAL      4    A (A**2):    265 ; 1.190 ; 0.500           
REMARK   3   MEDIUM THERMAL     4    A (A**2):    464 ; 1.760 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
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    80        A   304                          
REMARK   3    ORIGIN FOR THE GROUP (A):  58.2737  13.4945  16.3099              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2717 T22:   0.2462                                     
REMARK   3      T33:   0.3634 T12:   0.0338                                     
REMARK   3      T13:  -0.0940 T23:  -0.0330                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5902 L22:   0.9999                                     
REMARK   3      L33:   1.9611 L12:   1.2582                                     
REMARK   3      L13:   2.5545 L23:   0.5628                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0525 S12:   0.4035 S13:  -0.0559                       
REMARK   3      S21:  -0.3424 S22:   0.0787 S23:   0.3885                       
REMARK   3      S31:   0.0805 S32:  -0.0784 S33:  -0.0262                       
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   305        A   465                          
REMARK   3    ORIGIN FOR THE GROUP (A):  77.5741  12.2884  43.0839              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1409 T22:   0.1224                                     
REMARK   3      T33:   0.0594 T12:   0.0241                                     
REMARK   3      T13:  -0.0088 T23:  -0.0158                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.2130 L22:   6.0962                                     
REMARK   3      L33:   2.9080 L12:  -0.7513                                     
REMARK   3      L13:   0.1081 L23:  -0.7963                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1809 S12:  -0.5701 S13:  -0.2066                       
REMARK   3      S21:   0.7109 S22:   0.0594 S23:  -0.0315                       
REMARK   3      S31:   0.0957 S32:  -0.0498 S33:   0.1215                       
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 :   B    80        B   304                          
REMARK   3    ORIGIN FOR THE GROUP (A):  58.2196 -18.8993  52.4376              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3562 T22:   0.1795                                     
REMARK   3      T33:   0.3395 T12:  -0.0525                                     
REMARK   3      T13:   0.1781 T23:  -0.0639                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.3928 L22:   2.6993                                     
REMARK   3      L33:   1.6108 L12:  -0.0265                                     
REMARK   3      L13:  -1.9111 L23:  -0.1540                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2125 S12:  -0.4089 S13:   0.4801                       
REMARK   3      S21:   0.7543 S22:  -0.0347 S23:   0.8101                       
REMARK   3      S31:  -0.1970 S32:  -0.1107 S33:  -0.1778                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B   305        B   465                          
REMARK   3    ORIGIN FOR THE GROUP (A):  77.5653 -17.5646  25.7298              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1248 T22:   0.1260                                     
REMARK   3      T33:   0.0756 T12:   0.0068                                     
REMARK   3      T13:   0.0139 T23:  -0.0089                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.5099 L22:   6.2160                                     
REMARK   3      L33:   3.0664 L12:   1.3401                                     
REMARK   3      L13:  -0.8977 L23:  -1.0853                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1672 S12:   0.6054 S13:   0.2165                       
REMARK   3      S21:  -0.6989 S22:   0.0916 S23:  -0.2921                       
REMARK   3      S31:  -0.0731 S32:  -0.1827 S33:   0.0756                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5LXD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 21-SEP-16.                  
REMARK 100 THE DEPOSITION ID IS D_1200001519.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-DEC-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
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                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9200                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 35477                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.580                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.040                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.8                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.1000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.58                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.72                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.50                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.64900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.12                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.5 M LI2SO4 AND 0.1 M HEPES, PH 7.5,    
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277.15K                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
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   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        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  1.000000  0.000000  0.000000       33.12000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       65.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       33.12000            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       65.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     SER A    72                                                      
REMARK 465     MET A    73                                                      
REMARK 465     GLY A    74                                                      
REMARK 465     LYS A    75                                                      
REMARK 465     VAL A    76                                                      
REMARK 465     LYS A    77                                                      
REMARK 465     ALA A    78                                                      
REMARK 465     THR A    79                                                      
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 465     SER B    72                                                      
REMARK 465     MET B    73                                                      
REMARK 465     GLY B    74                                                      
REMARK 465     LYS B    75                                                      
REMARK 465     VAL B    76                                                      
REMARK 465     LYS B    77                                                      
REMARK 465     ALA B    78                                                      
REMARK 465     THR B    79                                                      
REMARK 465     LEU B   466                                                      
REMARK 465     PRO B   467                                                      
REMARK 465     LYS B   468                                                      
REMARK 465     PRO B   469                                                      
REMARK 465     PRO B   470                                                      
REMARK 465     THR B   471                                                      
REMARK 465     GLY B   472                                                      
REMARK 465     GLU B   473                                                      
REMARK 465     LYS B   474                                                      
REMARK 465     THR B   475                                                      
REMARK 465     SER B   476                                                      
REMARK 465     VAL B   477                                                      
REMARK 465     LYS B   478                                                      
REMARK 465     ARG B   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     MET A 121    SD   CE                                             
REMARK 470     GLN A 134    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 464    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 465    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET B 121    CG   SD   CE                                        
REMARK 470     GLN B 134    CG   CD   OE1  NE2                                  
REMARK 470     ARG B 464    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B 465    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OG   SER B   385     O1   EDO B   506              2.11            
REMARK 500   OG   SER A   385     O1   EDO A   506              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    SER A   398     NE2  GLN B   119     2756     2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A 146       47.41     36.83                                   
REMARK 500    TYR A 147       44.26     37.44                                   
REMARK 500    ARG A 148      -52.65   -150.51                                   
REMARK 500    HIS A 172       62.04     60.27                                   
REMARK 500    ARG A 181      156.83    -48.64                                   
REMARK 500    ASP A 204       53.05   -144.85                                   
REMARK 500    SER A 232     -150.12    -90.43                                   
REMARK 500    ASP A 275       46.58   -152.14                                   
REMARK 500    ASP A 295       85.87     67.75                                   
REMARK 500    GLN A 304       49.74   -101.89                                   
REMARK 500    GLN A 311      144.69     75.57                                   
REMARK 500    PRO A 350       77.39   -103.93                                   
REMARK 500    ALA B 146       45.74     39.24                                   
REMARK 500    TYR B 147       45.52     37.52                                   
REMARK 500    ARG B 148      -48.87   -151.87                                   
REMARK 500    ARG B 181      157.69    -48.87                                   
REMARK 500    ASP B 204       53.93   -144.85                                   
REMARK 500    SER B 232     -150.48    -87.54                                   
REMARK 500    ASP B 275       46.51   -155.73                                   
REMARK 500    ASP B 295       85.87     66.86                                   
REMARK 500    GLN B 304       50.36   -101.96                                   
REMARK 500    GLN B 311      145.14     73.17                                   
REMARK 500    PRO B 350       79.64   -105.64                                   
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 7A7 A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 506                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 7A7 B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 505                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 506                 
DBREF  5LXD A   73   479  UNP    Q92630   DYRK2_HUMAN    146    552             
DBREF  5LXD B   73   479  UNP    Q92630   DYRK2_HUMAN    146    552             
SEQADV 5LXD SER A   72  UNP  Q92630              EXPRESSION TAG                 
SEQADV 5LXD SER B   72  UNP  Q92630              EXPRESSION TAG                 
SEQRES   1 A  408  SER MET GLY LYS VAL LYS ALA THR PRO MET THR PRO GLU          
SEQRES   2 A  408  GLN ALA MET LYS GLN TYR MET GLN LYS LEU THR ALA PHE          
SEQRES   3 A  408  GLU HIS HIS GLU ILE PHE SER TYR PRO GLU ILE TYR PHE          
SEQRES   4 A  408  LEU GLY LEU ASN ALA LYS LYS ARG GLN GLY MET THR GLY          
SEQRES   5 A  408  GLY PRO ASN ASN GLY GLY TYR ASP ASP ASP GLN GLY SER          
SEQRES   6 A  408  TYR VAL GLN VAL PRO HIS ASP HIS VAL ALA TYR ARG TYR          
SEQRES   7 A  408  GLU VAL LEU LYS VAL ILE GLY LYS GLY SER PHE GLY GLN          
SEQRES   8 A  408  VAL VAL LYS ALA TYR ASP HIS LYS VAL HIS GLN HIS VAL          
SEQRES   9 A  408  ALA LEU LYS MET VAL ARG ASN GLU LYS ARG PHE HIS ARG          
SEQRES  10 A  408  GLN ALA ALA GLU GLU ILE ARG ILE LEU GLU HIS LEU ARG          
SEQRES  11 A  408  LYS GLN ASP LYS ASP ASN THR MET ASN VAL ILE HIS MET          
SEQRES  12 A  408  LEU GLU ASN PHE THR PHE ARG ASN HIS ILE CYS MET THR          
SEQRES  13 A  408  PHE GLU LEU LEU SER MET ASN LEU TYR GLU LEU ILE LYS          
SEQRES  14 A  408  LYS ASN LYS PHE GLN GLY PHE SER LEU PRO LEU VAL ARG          
SEQRES  15 A  408  LYS PHE ALA HIS SER ILE LEU GLN CYS LEU ASP ALA LEU          
SEQRES  16 A  408  HIS LYS ASN ARG ILE ILE HIS CYS ASP LEU LYS PRO GLU          
SEQRES  17 A  408  ASN ILE LEU LEU LYS GLN GLN GLY ARG SER GLY ILE LYS          
SEQRES  18 A  408  VAL ILE ASP PHE GLY SER SER CYS TYR GLU HIS GLN ARG          
SEQRES  19 A  408  VAL TYR THR PTR ILE GLN SER ARG PHE TYR ARG ALA PRO          
SEQRES  20 A  408  GLU VAL ILE LEU GLY ALA ARG TYR GLY MET PRO ILE ASP          
SEQRES  21 A  408  MET TRP SER LEU GLY CYS ILE LEU ALA GLU LEU LEU THR          
SEQRES  22 A  408  GLY TYR PRO LEU LEU PRO GLY GLU ASP GLU GLY ASP GLN          
SEQRES  23 A  408  LEU ALA CYS MET ILE GLU LEU LEU GLY MET PRO SER GLN          
SEQRES  24 A  408  LYS LEU LEU ASP ALA SER LYS ARG ALA LYS ASN PHE VAL          
SEQRES  25 A  408  SER SER LYS GLY TYR PRO ARG TYR CYS THR VAL THR THR          
SEQRES  26 A  408  LEU SER ASP GLY SER VAL VAL LEU ASN GLY GLY ARG SER          
SEQRES  27 A  408  ARG ARG GLY LYS LEU ARG GLY PRO PRO GLU SER ARG GLU          
SEQRES  28 A  408  TRP GLY ASN ALA LEU LYS GLY CYS ASP ASP PRO LEU PHE          
SEQRES  29 A  408  LEU ASP PHE LEU LYS GLN CYS LEU GLU TRP ASP PRO ALA          
SEQRES  30 A  408  VAL ARG MET THR PRO GLY GLN ALA LEU ARG HIS PRO TRP          
SEQRES  31 A  408  LEU ARG ARG ARG LEU PRO LYS PRO PRO THR GLY GLU LYS          
SEQRES  32 A  408  THR SER VAL LYS ARG                                          
SEQRES   1 B  408  SER MET GLY LYS VAL LYS ALA THR PRO MET THR PRO GLU          
SEQRES   2 B  408  GLN ALA MET LYS GLN TYR MET GLN LYS LEU THR ALA PHE          
SEQRES   3 B  408  GLU HIS HIS GLU ILE PHE SER TYR PRO GLU ILE TYR PHE          
SEQRES   4 B  408  LEU GLY LEU ASN ALA LYS LYS ARG GLN GLY MET THR GLY          
SEQRES   5 B  408  GLY PRO ASN ASN GLY GLY TYR ASP ASP ASP GLN GLY SER          
SEQRES   6 B  408  TYR VAL GLN VAL PRO HIS ASP HIS VAL ALA TYR ARG TYR          
SEQRES   7 B  408  GLU VAL LEU LYS VAL ILE GLY LYS GLY SER PHE GLY GLN          
SEQRES   8 B  408  VAL VAL LYS ALA TYR ASP HIS LYS VAL HIS GLN HIS VAL          
SEQRES   9 B  408  ALA LEU LYS MET VAL ARG ASN GLU LYS ARG PHE HIS ARG          
SEQRES  10 B  408  GLN ALA ALA GLU GLU ILE ARG ILE LEU GLU HIS LEU ARG          
SEQRES  11 B  408  LYS GLN ASP LYS ASP ASN THR MET ASN VAL ILE HIS MET          
SEQRES  12 B  408  LEU GLU ASN PHE THR PHE ARG ASN HIS ILE CYS MET THR          
SEQRES  13 B  408  PHE GLU LEU LEU SER MET ASN LEU TYR GLU LEU ILE LYS          
SEQRES  14 B  408  LYS ASN LYS PHE GLN GLY PHE SER LEU PRO LEU VAL ARG          
SEQRES  15 B  408  LYS PHE ALA HIS SER ILE LEU GLN CYS LEU ASP ALA LEU          
SEQRES  16 B  408  HIS LYS ASN ARG ILE ILE HIS CYS ASP LEU LYS PRO GLU          
SEQRES  17 B  408  ASN ILE LEU LEU LYS GLN GLN GLY ARG SER GLY ILE LYS          
SEQRES  18 B  408  VAL ILE ASP PHE GLY SER SER CYS TYR GLU HIS GLN ARG          
SEQRES  19 B  408  VAL TYR THR PTR ILE GLN SER ARG PHE TYR ARG ALA PRO          
SEQRES  20 B  408  GLU VAL ILE LEU GLY ALA ARG TYR GLY MET PRO ILE ASP          
SEQRES  21 B  408  MET TRP SER LEU GLY CYS ILE LEU ALA GLU LEU LEU THR          
SEQRES  22 B  408  GLY TYR PRO LEU LEU PRO GLY GLU ASP GLU GLY ASP GLN          
SEQRES  23 B  408  LEU ALA CYS MET ILE GLU LEU LEU GLY MET PRO SER GLN          
SEQRES  24 B  408  LYS LEU LEU ASP ALA SER LYS ARG ALA LYS ASN PHE VAL          
SEQRES  25 B  408  SER SER LYS GLY TYR PRO ARG TYR CYS THR VAL THR THR          
SEQRES  26 B  408  LEU SER ASP GLY SER VAL VAL LEU ASN GLY GLY ARG SER          
SEQRES  27 B  408  ARG ARG GLY LYS LEU ARG GLY PRO PRO GLU SER ARG GLU          
SEQRES  28 B  408  TRP GLY ASN ALA LEU LYS GLY CYS ASP ASP PRO LEU PHE          
SEQRES  29 B  408  LEU ASP PHE LEU LYS GLN CYS LEU GLU TRP ASP PRO ALA          
SEQRES  30 B  408  VAL ARG MET THR PRO GLY GLN ALA LEU ARG HIS PRO TRP          
SEQRES  31 B  408  LEU ARG ARG ARG LEU PRO LYS PRO PRO THR GLY GLU LYS          
SEQRES  32 B  408  THR SER VAL LYS ARG                                          
MODRES 5LXD PTR A  309  TYR  MODIFIED RESIDUE                                   
MODRES 5LXD PTR B  309  TYR  MODIFIED RESIDUE                                   
HET    PTR  A 309      16                                                       
HET    PTR  B 309      16                                                       
HET    7A7  A 501      27                                                       
HET    EDO  A 502       4                                                       
HET    EDO  A 503       4                                                       
HET    EDO  A 504       4                                                       
HET    EDO  A 505       4                                                       
HET    EDO  A 506       4                                                       
HET    7A7  B 501      27                                                       
HET    EDO  B 502       4                                                       
HET    EDO  B 503       4                                                       
HET    EDO  B 504       4                                                       
HET    EDO  B 505       4                                                       
HET    EDO  B 506       4                                                       
HETNAM     PTR O-PHOSPHOTYROSINE                                                
HETNAM     7A7 METHYL 9-[(2-FLUORANYL-4-METHOXY-PHENYL)AMINO]-[1,               
HETNAM   2 7A7  3]THIAZOLO[5,4-F]QUINAZOLINE-2-CARBOXIMIDATE                    
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     PTR PHOSPHONOTYROSINE                                                
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  PTR    2(C9 H12 N O6 P)                                             
FORMUL   3  7A7    2(C18 H14 F N5 O2 S)                                         
FORMUL   4  EDO    10(C2 H6 O2)                                                 
FORMUL  15  HOH   *193(H2 O)                                                    
HELIX    1 AA1 THR A   82  MET A   91  1                                  10    
HELIX    2 AA2 GLN A   92  LEU A   94  5                                   3    
HELIX    3 AA3 THR A   95  ILE A  102  1                                   8    
HELIX    4 AA4 PHE A  103  TYR A  105  5                                   3    
HELIX    5 AA5 GLY A  124  TYR A  130  1                                   7    
HELIX    6 AA6 GLU A  183  LYS A  202  1                                  20    
HELIX    7 AA7 ASN A  234  ASN A  242  1                                   9    
HELIX    8 AA8 SER A  248  ASN A  269  1                                  22    
HELIX    9 AA9 LYS A  277  GLU A  279  5                                   3    
HELIX   10 AB1 SER A  312  ARG A  316  5                                   5    
HELIX   11 AB2 ALA A  317  GLY A  323  1                                   7    
HELIX   12 AB3 PRO A  329  GLY A  345  1                                  17    
HELIX   13 AB4 ASP A  353  GLY A  366  1                                  14    
HELIX   14 AB5 SER A  369  ALA A  375  1                                   7    
HELIX   15 AB6 ARG A  378  VAL A  383  1                                   6    
HELIX   16 AB7 GLU A  422  LEU A  427  1                                   6    
HELIX   17 AB8 ASP A  432  LEU A  443  1                                  12    
HELIX   18 AB9 THR A  452  HIS A  459  1                                   8    
HELIX   19 AC1 PRO A  460  ARG A  463  5                                   4    
HELIX   20 AC2 THR B   82  MET B   91  1                                  10    
HELIX   21 AC3 GLN B   92  LEU B   94  5                                   3    
HELIX   22 AC4 THR B   95  ILE B  102  1                                   8    
HELIX   23 AC5 PHE B  103  TYR B  105  5                                   3    
HELIX   24 AC6 GLY B  124  TYR B  130  1                                   7    
HELIX   25 AC7 GLU B  183  LYS B  202  1                                  20    
HELIX   26 AC8 ASN B  234  ASN B  242  1                                   9    
HELIX   27 AC9 SER B  248  ASN B  269  1                                  22    
HELIX   28 AD1 LYS B  277  GLU B  279  5                                   3    
HELIX   29 AD2 SER B  312  ARG B  316  5                                   5    
HELIX   30 AD3 ALA B  317  GLY B  323  1                                   7    
HELIX   31 AD4 PRO B  329  GLY B  345  1                                  17    
HELIX   32 AD5 ASP B  353  GLY B  366  1                                  14    
HELIX   33 AD6 SER B  369  ALA B  375  1                                   7    
HELIX   34 AD7 ARG B  378  VAL B  383  1                                   6    
HELIX   35 AD8 GLU B  422  LEU B  427  1                                   6    
HELIX   36 AD9 ASP B  432  LEU B  443  1                                  12    
HELIX   37 AE1 THR B  452  ARG B  458  1                                   7    
HELIX   38 AE2 HIS B  459  ARG B  463  5                                   5    
SHEET    1 AA1 6 HIS A 144  VAL A 145  0                                        
SHEET    2 AA1 6 TYR A 149  GLY A 158 -1  O  TYR A 149   N  VAL A 145           
SHEET    3 AA1 6 GLY A 161  ASP A 168 -1  O  VAL A 163   N  GLY A 156           
SHEET    4 AA1 6 GLN A 173  VAL A 180 -1  O  VAL A 175   N  ALA A 166           
SHEET    5 AA1 6 HIS A 223  PHE A 228 -1  O  MET A 226   N  LYS A 178           
SHEET    6 AA1 6 MET A 214  PHE A 220 -1  N  PHE A 218   O  CYS A 225           
SHEET    1 AA2 2 ILE A 271  ILE A 272  0                                        
SHEET    2 AA2 2 CYS A 300  TYR A 301 -1  O  CYS A 300   N  ILE A 272           
SHEET    1 AA3 2 ILE A 281  LEU A 283  0                                        
SHEET    2 AA3 2 ILE A 291  VAL A 293 -1  O  LYS A 292   N  LEU A 282           
SHEET    1 AA4 2 THR A 393  THR A 396  0                                        
SHEET    2 AA4 2 VAL A 402  ASN A 405 -1  O  ASN A 405   N  THR A 393           
SHEET    1 AA5 2 GLY A 407  ARG A 408  0                                        
SHEET    2 AA5 2 LEU A 414  ARG A 415 -1  O  ARG A 415   N  GLY A 407           
SHEET    1 AA6 6 HIS B 144  VAL B 145  0                                        
SHEET    2 AA6 6 TYR B 149  GLY B 158 -1  O  TYR B 149   N  VAL B 145           
SHEET    3 AA6 6 GLY B 161  ASP B 168 -1  O  VAL B 163   N  GLY B 156           
SHEET    4 AA6 6 GLN B 173  VAL B 180 -1  O  LEU B 177   N  VAL B 164           
SHEET    5 AA6 6 HIS B 223  PHE B 228 -1  O  MET B 226   N  LYS B 178           
SHEET    6 AA6 6 MET B 214  PHE B 220 -1  N  LEU B 215   O  THR B 227           
SHEET    1 AA7 2 ILE B 271  ILE B 272  0                                        
SHEET    2 AA7 2 CYS B 300  TYR B 301 -1  O  CYS B 300   N  ILE B 272           
SHEET    1 AA8 2 ILE B 281  LEU B 283  0                                        
SHEET    2 AA8 2 ILE B 291  VAL B 293 -1  O  LYS B 292   N  LEU B 282           
SHEET    1 AA9 2 THR B 393  THR B 396  0                                        
SHEET    2 AA9 2 VAL B 402  ASN B 405 -1  O  VAL B 403   N  THR B 395           
SHEET    1 AB1 2 GLY B 407  ARG B 408  0                                        
SHEET    2 AB1 2 LEU B 414  ARG B 415 -1  O  ARG B 415   N  GLY B 407           
LINK         C   THR A 308                 N   PTR A 309     1555   1555  1.33  
LINK         C   PTR A 309                 N   ILE A 310     1555   1555  1.32  
LINK         C   THR B 308                 N   PTR B 309     1555   1555  1.33  
LINK         C   PTR B 309                 N   ILE B 310     1555   1555  1.32  
SITE     1 AC1 13 GLY A 156  LYS A 157  PHE A 160  VAL A 163                    
SITE     2 AC1 13 ALA A 176  LYS A 178  ILE A 212  PHE A 228                    
SITE     3 AC1 13 GLU A 229  LEU A 231  LEU A 282  ILE A 294                    
SITE     4 AC1 13 ASP A 295                                                     
SITE     1 AC2  1 ASN A 381                                                     
SITE     1 AC3  2 ARG A 421  ASN A 425                                          
SITE     1 AC4  1 ARG A 458                                                     
SITE     1 AC5  2 ARG A 288  GLY A 290                                          
SITE     1 AC6  3 SER A 384  SER A 385  ARG A 390                               
SITE     1 AC7 14 GLY B 156  LYS B 157  PHE B 160  VAL B 163                    
SITE     2 AC7 14 ALA B 176  LYS B 178  ILE B 212  PHE B 228                    
SITE     3 AC7 14 GLU B 229  LEU B 231  ASN B 280  LEU B 282                    
SITE     4 AC7 14 ILE B 294  ASP B 295                                          
SITE     1 AC8  1 THR B 308                                                     
SITE     1 AC9  2 ARG B 378  ASN B 381                                          
SITE     1 AD1  3 ARG B 421  ASN B 425  HOH B 642                               
SITE     1 AD2  2 ARG B 288  GLY B 290                                          
SITE     1 AD3  3 SER B 384  SER B 385  ARG B 390                               
CRYST1   66.240  130.000  136.330  90.00  90.40  90.00 C 1 2 1       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      0.015097  0.000000  0.000105        0.00000                         
SCALE2      0.000000  0.007692  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007335        0.00000                         
MTRIX1   1  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   1  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   1  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   2  0.999863  0.001153  0.016514       -0.78145    1                    
MTRIX2   2  0.001202 -0.999995 -0.002972       -5.30909    1                    
MTRIX3   2  0.016511  0.002992 -0.999859       67.85150    1                    
MTRIX1   3  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   3  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   3  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   4  0.999996  0.002860  0.000148        0.05665    1                    
MTRIX2   4  0.002860 -0.999994 -0.002175       -5.44937    1                    
MTRIX3   4  0.000141  0.002175 -0.999998       68.87262    1                    
MTRIX1   5  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   5  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   5  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   6  0.999981  0.005646  0.002275        0.01857    1                    
MTRIX2   6  0.005664 -0.999951 -0.008140       -5.52643    1                    
MTRIX3   6  0.002229  0.008153 -0.999964       68.65328    1                    
MTRIX1   7  1.000000  0.000000  0.000000        0.00000    1                    
MTRIX2   7  0.000000  1.000000  0.000000        0.00000    1                    
MTRIX3   7  0.000000  0.000000  1.000000        0.00000    1                    
MTRIX1   8  0.999990 -0.002367 -0.003707        0.05027    1                    
MTRIX2   8 -0.002367 -0.999997 -0.000009       -5.12866    1                    
MTRIX3   8 -0.003707  0.000017 -0.999993       69.09409    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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