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Database: PDB
Entry: 4UMT
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Original site: 4UMT 
HEADER    TRANSFERASE                             21-MAY-14   4UMT              
TITLE     STRUCTURE OF MELK IN COMPLEX WITH INHIBITORS                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MATERNAL EMBRYONIC LEUCINE ZIPPER KINASE;                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HMELK, PROTEIN KINASE EG3, PEG3 KINASE, PROTEIN KINASE      
COMPND   5  PK38, HPK38, TYROSINE-PROTEIN KINASE MELK;                          
COMPND   6 EC: 2.7.11.1, 2.7.10.2;                                              
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: 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 OTHER_DETAILS: IMAGE CLONE                                           
KEYWDS    TRANSFERASE, FRAGMENT BASED DRUG DESIGN                               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.N.JOHNSON,V.BERDINI,L.BEKE,P.BONNET,D.BREHMER,J.E.COYLE,P.J.DAY,    
AUTHOR   2 M.FREDERICKSON,E.J.E.FREYNE,R.A.H.J.GILISSEN,C.C.F.HAMLETT,S.HOWARD, 
AUTHOR   3 L.MEERPOEL,R.MCMENAMIN,S.PATEL,D.C.REES,A.SHARFF,F.SOMMEN,T.WU,      
AUTHOR   4 J.T.M.LINDERS                                                        
REVDAT   2   28-JAN-15 4UMT    1       JRNL                                     
REVDAT   1   22-OCT-14 4UMT    0                                                
JRNL        AUTH   C.N.JOHNSON,C.ADELINET,V.BERDINI,L.BEKE,P.BONNET,D.BREHMER,  
JRNL        AUTH 2 F.CALO,J.E.COYLE,P.J.DAY,M.FREDERICKSON,E.J.E.FREYNE,        
JRNL        AUTH 3 R.A.H.J.GILISSEN,C.C.F.HAMLETT,S.HOWARD,L.MEERPOEL,          
JRNL        AUTH 4 L.MEVELLEC,R.MCMENAMIN,E.PASQUIER,S.PATEL,D.C.REES,          
JRNL        AUTH 5 J.T.M.LINDERS                                                
JRNL        TITL   STRUCTURE-BASED DESIGN OF TYPE II INHIBITORS APPLIED TO      
JRNL        TITL 2 MATERNAL EMBRYONIC LEUCINE ZIPPER KINASE.                    
JRNL        REF    ACS MED.CHEM.LETT.            V.   6    31 2015              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   25589926                                                     
JRNL        DOI    10.1021/ML5001273                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.98 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0064                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,                      
REMARK   3                 STEINER,NICHOLLS,WINN,LONG,VAGIN                     
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.98                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 89.44                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NONE                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.11                          
REMARK   3   NUMBER OF REFLECTIONS             : 26683                          
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) : 0.21442                         
REMARK   3   R VALUE            (WORKING SET) : 0.21326                         
REMARK   3   FREE R VALUE                     : 0.23644                         
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.9                             
REMARK   3   FREE R VALUE TEST SET COUNT      : 1388                            
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) : 1.975                        
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.026                        
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1942                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.94                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.303                        
REMARK   3   BIN FREE R VALUE SET COUNT          : 112                          
REMARK   3   BIN FREE R VALUE                    : 0.339                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2565                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 198                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 47.204                         
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00                                                 
REMARK   3    B22 (A**2) : 0.00                                                 
REMARK   3    B33 (A**2) : 0.00                                                 
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): 0.182         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.154         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2659 ; 0.011 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2577 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3596 ; 1.364 ; 1.963       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5932 ; 3.568 ; 2.980       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   314 ; 5.508 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   122 ;36.694 ;23.918       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   485 ;16.841 ;15.031       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;20.052 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   396 ; 0.082 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2922 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   604 ; 0.003 ; 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):  1262 ; 2.001 ;10.985       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1261 ; 1.995 ;10.981       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1397 ; 2.422 ;11.167       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1398 ; 2.422 ;11.165       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):   935 ; 5.176 ;23.938       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):   926 ; 5.200 ;23.990       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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. U VALUES REFINED INDIVIDUALLY.                   
REMARK   4                                                                      
REMARK   4 4UMT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-SEP-14.                  
REMARK 100 THE PDBE ID CODE IS EBI-60712.                                       
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-JUN-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97                               
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 : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 28321                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.98                               
REMARK 200  RESOLUTION RANGE LOW       (A) : 89.99                              
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.0                                
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.1                               
REMARK 200  DATA REDUNDANCY                : 3.5                                
REMARK 200  R MERGE                    (I) : 0.04                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 2.40                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: OTHER                        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 60                                        
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.1                      
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       21.62900            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       43.25800            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       43.25800            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       21.62900            
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 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   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 465     CYS A   154                                                      
REMARK 465     ALA A   155                                                      
REMARK 465     LYS A   156                                                      
REMARK 465     PRO A   157                                                      
REMARK 465     LYS A   158                                                      
REMARK 465     GLY A   159                                                      
REMARK 465     ASN A   160                                                      
REMARK 465     LYS A   161                                                      
REMARK 465     ASP A   162                                                      
REMARK 465     TYR A   163                                                      
REMARK 465     HIS A   164                                                      
REMARK 465     LEU A   165                                                      
REMARK 465     GLN A   166                                                      
REMARK 465     THR A   167                                                      
REMARK 465     CYS A   168                                                      
REMARK 465     LEU A   334                                                      
REMARK 465     SER A   335                                                      
REMARK 465     SER A   336                                                      
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   O    HOH A  2018     O    HOH A  2079              1.27            
REMARK 500   O    HOH A  2019     O    HOH A  2083              1.79            
REMARK 500   O    HOH A  2086     O    HOH A  2089              2.02            
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    HOH A  2045     O    HOH A  2181     3665     2.13            
REMARK 500   O    HOH A  2078     O    HOH A  2102     5555     0.93            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    LEU A 217   C     VAL A 218   N      -0.167                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 251   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG A 251   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    HIS A  14     -159.17   -110.76                                   
REMARK 500    THR A  78     -168.74   -129.68                                   
REMARK 500    ASP A 102      -69.87     79.97                                   
REMARK 500    ARG A 131       -2.05     79.99                                   
REMARK 500    ASP A 132       48.33   -142.55                                   
REMARK 500    LEU A 244       54.55   -103.86                                   
REMARK 500    ILE A 280      -88.25   -104.04                                   
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 DMS A1334                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 47W A1335                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4UMP   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF MELK IN COMPLEX WITH INHIBITORS                        
REMARK 900 RELATED ID: 4UMQ   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF MELK IN COMPLEX WITH INHIBITORS                        
REMARK 900 RELATED ID: 4UMR   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF MELK IN COMPLEX WITH INHIBITORS                        
REMARK 900 RELATED ID: 4UMU   RELATED DB: PDB                                   
REMARK 900  STRUCTURE OF MELK IN COMPLEX WITH INHIBITORS                        
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 POINT MUTATIONS AND HIS TAG ARE PRESENT                              
DBREF  4UMT A    1   336  UNP    Q14680   MELK_HUMAN       1    336             
SEQADV 4UMT MET A  -19  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMT GLY A  -18  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMT SER A  -17  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMT SER A  -16  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMT HIS A  -15  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMT HIS A  -14  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMT HIS A  -13  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMT HIS A  -12  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMT HIS A  -11  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMT HIS A  -10  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMT SER A   -9  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMT SER A   -8  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMT GLY A   -7  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMT LEU A   -6  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMT VAL A   -5  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMT PRO A   -4  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMT ARG A   -3  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMT GLY A   -2  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMT SER A   -1  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMT HIS A    0  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMT THR A  213  UNP  Q14680    ASN   213 ENGINEERED MUTATION            
SEQADV 4UMT ALA A  214  UNP  Q14680    VAL   214 ENGINEERED MUTATION            
SEQADV 4UMT ALA A  215  UNP  Q14680    MET   215 ENGINEERED MUTATION            
SEQADV 4UMT VAL A  218  UNP  Q14680    TYR   218 ENGINEERED MUTATION            
SEQADV 4UMT ALA A  219  UNP  Q14680    LYS   219 ENGINEERED MUTATION            
SEQRES   1 A  356  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  356  LEU VAL PRO ARG GLY SER HIS MET LYS ASP TYR ASP GLU          
SEQRES   3 A  356  LEU LEU LYS TYR TYR GLU LEU HIS GLU THR ILE GLY THR          
SEQRES   4 A  356  GLY GLY PHE ALA LYS VAL LYS LEU ALA CYS HIS ILE LEU          
SEQRES   5 A  356  THR GLY GLU MET VAL ALA ILE LYS ILE MET ASP LYS ASN          
SEQRES   6 A  356  THR LEU GLY SER ASP LEU PRO ARG ILE LYS THR GLU ILE          
SEQRES   7 A  356  GLU ALA LEU LYS ASN LEU ARG HIS GLN HIS ILE CYS GLN          
SEQRES   8 A  356  LEU TYR HIS VAL LEU GLU THR ALA ASN LYS ILE PHE MET          
SEQRES   9 A  356  VAL LEU GLU TYR CYS PRO GLY GLY GLU LEU PHE ASP TYR          
SEQRES  10 A  356  ILE ILE SER GLN ASP ARG LEU SER GLU GLU GLU THR ARG          
SEQRES  11 A  356  VAL VAL PHE ARG GLN ILE VAL SER ALA VAL ALA TYR VAL          
SEQRES  12 A  356  HIS SER GLN GLY TYR ALA HIS ARG ASP LEU LYS PRO GLU          
SEQRES  13 A  356  ASN LEU LEU PHE ASP GLU TYR HIS LYS LEU LYS LEU ILE          
SEQRES  14 A  356  ASP PHE GLY LEU CYS ALA LYS PRO LYS GLY ASN LYS ASP          
SEQRES  15 A  356  TYR HIS LEU GLN THR CYS CYS GLY SER LEU ALA TYR ALA          
SEQRES  16 A  356  ALA PRO GLU LEU ILE GLN GLY LYS SER TYR LEU GLY SER          
SEQRES  17 A  356  GLU ALA ASP VAL TRP SER MET GLY ILE LEU LEU TYR VAL          
SEQRES  18 A  356  LEU MET CYS GLY PHE LEU PRO PHE ASP ASP ASP THR ALA          
SEQRES  19 A  356  ALA ALA LEU VAL ALA LYS ILE MET ARG GLY LYS TYR ASP          
SEQRES  20 A  356  VAL PRO LYS TRP LEU SER PRO SER SER ILE LEU LEU LEU          
SEQRES  21 A  356  GLN GLN MET LEU GLN VAL ASP PRO LYS LYS ARG ILE SER          
SEQRES  22 A  356  MET LYS ASN LEU LEU ASN HIS PRO TRP ILE MET GLN ASP          
SEQRES  23 A  356  TYR ASN TYR PRO VAL GLU TRP GLN SER LYS ASN PRO PHE          
SEQRES  24 A  356  ILE HIS LEU ASP ASP ASP CYS VAL THR GLU LEU SER VAL          
SEQRES  25 A  356  HIS HIS ARG ASN ASN ARG GLN THR MET GLU ASP LEU ILE          
SEQRES  26 A  356  SER LEU TRP GLN TYR ASP HIS LEU THR ALA THR TYR LEU          
SEQRES  27 A  356  LEU LEU LEU ALA LYS LYS ALA ARG GLY LYS PRO VAL ARG          
SEQRES  28 A  356  LEU ARG LEU SER SER                                          
HET    DMS  A1334       4                                                       
HET    47W  A1335      56                                                       
HETNAM     47W 1-(4-{[3-(ISOQUINOLIN-7-YL)PROP-2-YN-1-YL]                       
HETNAM   2 47W  OXY}-2-METHOXYBENZYL)PIPERAZINEDIIUM                            
HETNAM     DMS DIMETHYL SULFOXIDE                                               
FORMUL   2  47W    C24 H27 N3 O2 2+                                             
FORMUL   3  DMS    C2 H6 O S                                                    
FORMUL   4  HOH   *198(H2 O)                                                    
HELIX    1   1 GLU A    6  TYR A   10  1                                   5    
HELIX    2   2 LYS A   44  GLY A   48  1                                   5    
HELIX    3   3 ASP A   50  ASN A   63  1                                  14    
HELIX    4   4 LEU A   94  ASP A  102  1                                   9    
HELIX    5   5 SER A  105  GLN A  126  1                                  22    
HELIX    6   6 LYS A  134  GLU A  136  5                                   3    
HELIX    7   7 CYS A  169  ALA A  175  5                                   7    
HELIX    8   8 ALA A  176  GLN A  181  1                                   6    
HELIX    9   9 LEU A  186  GLY A  205  1                                  20    
HELIX   10  10 THR A  213  GLY A  224  1                                  12    
HELIX   11  11 SER A  233  LEU A  244  1                                  12    
HELIX   12  12 ASP A  247  ARG A  251  5                                   5    
HELIX   13  13 SER A  253  ASN A  259  1                                   7    
HELIX   14  14 ASP A  283  ARG A  295  1                                  13    
HELIX   15  15 ASN A  297  SER A  306  1                                  10    
HELIX   16  16 ASP A  311  ARG A  326  1                                  16    
SHEET    1  AA 5 TYR A  11  GLY A  18  0                                        
SHEET    2  AA 5 ALA A  23  HIS A  30 -1  O  VAL A  25   N  ILE A  17           
SHEET    3  AA 5 GLU A  35  ASP A  43 -1  O  GLU A  35   N  HIS A  30           
SHEET    4  AA 5 LYS A  81  GLU A  87 -1  O  ILE A  82   N  MET A  42           
SHEET    5  AA 5 LEU A  72  GLU A  77 -1  N  TYR A  73   O  VAL A  85           
SHEET    1  AB 3 GLY A  92  GLU A  93  0                                        
SHEET    2  AB 3 LEU A 138  PHE A 140 -1  N  PHE A 140   O  GLY A  92           
SHEET    3  AB 3 LEU A 146  LEU A 148 -1  O  LYS A 147   N  LEU A 139           
SITE     1 AC1  6 GLU A  35  MET A  36  TYR A  73  ALA A 322                    
SITE     2 AC1  6 ARG A 326  HOH A2015                                          
SITE     1 AC2 13 ALA A  38  GLU A  57  ALA A  60  ILE A  69                    
SITE     2 AC2 13 GLU A  87  CYS A  89  ALA A 129  HIS A 130                    
SITE     3 AC2 13 LEU A 139  ILE A 149  ASP A 150  HOH A2027                    
SITE     4 AC2 13 HOH A2198                                                     
CRYST1  103.274  103.274   64.887  90.00  90.00 120.00 P 31 2 1      6          
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      0.009683  0.005590  0.000000        0.00000                         
SCALE2      0.000000  0.011181  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015411        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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