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Database: PDB
Entry: 4UMP
LinkDB: 4UMP
Original site: 4UMP 
HEADER    TRANSFERASE                             20-MAY-14   4UMP              
TITLE     STRUCTURE OF MELK IN COMPLEX WITH INHIBITORS                          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MATERNAL EMBRYONIC LEUCINE ZIPPER KINASE;                  
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: HMELK, PROTEIN KINASE EG3, PEG3 KINASE, PROTEIN KINASE PK38,
COMPND   5 HPK38, TYROSINE-PROTEIN KINASE MELK, 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                                                           
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   3   04-APR-18 4UMP    1       REMARK                                   
REVDAT   2   28-JAN-15 4UMP    1       JRNL                                     
REVDAT   1   08-OCT-14 4UMP    0                                                
JRNL        AUTH   C.N.JOHNSON,V.BERDINI,L.BEKE,P.BONNET,D.BREHMER,J.E.COYLE,   
JRNL        AUTH 2 P.J.DAY,M.FREDERICKSON,E.J.E.FREYNE,R.A.H.J.GILISSEN,        
JRNL        AUTH 3 C.C.F.HAMLETT,S.HOWARD,L.MEERPOEL,R.MCMENAMIN,S.PATEL,       
JRNL        AUTH 4 D.C.REES,A.SHARFF,F.SOMMEN,T.WU,J.T.M.LINDERS                
JRNL        TITL   FRAGMENT-BASED DISCOVERY OF TYPE I INHIBITORS OF MATERNAL    
JRNL        TITL 2 EMBRYONIC LEUCINE ZIPPER KINASE                              
JRNL        REF    ACS MED.CHEM.LETT.            V.   6    25 2015              
JRNL        REFN                   ISSN 1948-5875                               
JRNL        PMID   25589925                                                     
JRNL        DOI    10.1021/ML5001245                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.5                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.38                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 58731                          
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)  : 0.238                          
REMARK   3   R VALUE            (WORKING SET)  : 0.235                          
REMARK   3   FREE R VALUE                      : 0.291                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.090                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 2989                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 20                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.30                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.36                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 95.71                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 4233                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2625                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 4001                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2594                   
REMARK   3   BIN FREE R VALUE                        : 0.3176                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.48                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 232                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10268                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 564                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 62.93                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 61.08                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.48010                                              
REMARK   3    B22 (A**2) : -1.70190                                             
REMARK   3    B33 (A**2) : -3.77820                                             
REMARK   3    B12 (A**2) : -1.64770                                             
REMARK   3    B13 (A**2) : 3.84620                                              
REMARK   3    B23 (A**2) : -2.88550                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.424               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.448               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.285               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.467               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.292               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.919                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.885                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 10612  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 14365  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 3724   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 254    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1533   ; 16.000 ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 10612  ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 1338   ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 12136  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.011                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.94                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 6.91                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 21.02                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A):    8.7193   -0.8056  -12.2074           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0848 T22:    0.0236                                    
REMARK   3     T33:   -0.0105 T12:    0.1616                                    
REMARK   3     T13:    0.0222 T23:    0.0649                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.8643 L22:    0.1672                                    
REMARK   3     L33:    1.3889 L12:    0.4805                                    
REMARK   3     L13:   -1.0745 L23:    1.1993                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0072 S12:    0.0058 S13:    0.0115                     
REMARK   3     S21:   -0.0272 S22:   -0.0131 S23:   -0.0198                     
REMARK   3     S31:   -0.0125 S32:    0.0365 S33:    0.0203                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -11.2817    3.7285    5.9685           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0053 T22:   -0.0097                                    
REMARK   3     T33:   -0.1290 T12:    0.1348                                    
REMARK   3     T13:    0.0538 T23:    0.0454                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.9857 L22:    0.8898                                    
REMARK   3     L33:    0.2689 L12:   -0.7045                                    
REMARK   3     L13:   -0.2157 L23:    0.1391                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0122 S12:   -0.1185 S13:    0.0400                     
REMARK   3     S21:    0.0217 S22:    0.0557 S23:    0.0401                     
REMARK   3     S31:    0.0032 S32:   -0.0101 S33:   -0.0435                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A):   19.6279  -11.7041   -0.8127           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0449 T22:    0.0537                                    
REMARK   3     T33:   -0.0175 T12:    0.1694                                    
REMARK   3     T13:   -0.0858 T23:    0.0920                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.7762 L22:    0.1176                                    
REMARK   3     L33:    0.0299 L12:   -1.7479                                    
REMARK   3     L13:    0.8226 L23:   -0.8181                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0055 S12:   -0.0242 S13:   -0.0175                     
REMARK   3     S21:    0.0308 S22:   -0.0133 S23:   -0.0057                     
REMARK   3     S31:    0.0212 S32:    0.0376 S33:    0.0078                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A):   -2.9540  -33.9930  -20.9811           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0958 T22:    0.0159                                    
REMARK   3     T33:    0.0372 T12:    0.0308                                    
REMARK   3     T13:   -0.0238 T23:    0.0407                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.5781 L22:    0.0666                                    
REMARK   3     L33:    1.5158 L12:   -0.0654                                    
REMARK   3     L13:   -1.3231 L23:   -0.3442                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0059 S12:   -0.0108 S13:    0.0066                     
REMARK   3     S21:   -0.0315 S22:   -0.0120 S23:    0.0045                     
REMARK   3     S31:   -0.0357 S32:    0.0266 S33:    0.0180                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -23.1342  -35.1240   -2.7295           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1294 T22:   -0.0926                                    
REMARK   3     T33:    0.1008 T12:    0.0968                                    
REMARK   3     T13:   -0.0330 T23:    0.0006                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.3865 L22:    0.8329                                    
REMARK   3     L33:    1.7646 L12:    0.2516                                    
REMARK   3     L13:   -0.7656 L23:   -0.3454                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0076 S12:   -0.0267 S13:    0.0276                     
REMARK   3     S21:    0.0197 S22:    0.0222 S23:    0.0795                     
REMARK   3     S31:   -0.0351 S32:   -0.0009 S33:   -0.0146                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A):   10.8115  -40.2229   -9.0877           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1037 T22:    0.0889                                    
REMARK   3     T33:    0.0023 T12:   -0.0093                                    
REMARK   3     T13:   -0.0696 T23:    0.0770                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.7852 L22:   -0.0513                                    
REMARK   3     L33:   -0.6178 L12:    0.0358                                    
REMARK   3     L13:    0.9360 L23:   -0.7278                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0035 S12:   -0.0213 S13:   -0.0051                     
REMARK   3     S21:    0.0215 S22:    0.0102 S23:   -0.0003                     
REMARK   3     S31:    0.0018 S32:    0.0255 S33:   -0.0067                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -26.8451  -38.5776  -30.9868           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1090 T22:   -0.0220                                    
REMARK   3     T33:    0.0774 T12:   -0.0250                                    
REMARK   3     T13:   -0.0258 T23:    0.0233                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.4477 L22:    0.1556                                    
REMARK   3     L33:    1.0049 L12:   -0.4919                                    
REMARK   3     L13:   -0.5086 L23:   -0.3443                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0029 S12:   -0.0229 S13:    0.0032                     
REMARK   3     S21:    0.0267 S22:    0.0014 S23:    0.0105                     
REMARK   3     S31:    0.0124 S32:   -0.0033 S33:   -0.0043                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A):   -6.6808  -32.6362  -48.6724           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0351 T22:   -0.0732                                    
REMARK   3     T33:    0.0128 T12:    0.0521                                    
REMARK   3     T13:   -0.0418 T23:   -0.0338                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.8092 L22:    0.2839                                    
REMARK   3     L33:    0.9701 L12:    0.5935                                    
REMARK   3     L13:   -0.0614 L23:   -0.0834                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0481 S12:    0.1501 S13:   -0.0811                     
REMARK   3     S21:   -0.0210 S22:    0.0923 S23:   -0.0133                     
REMARK   3     S31:   -0.0214 S32:   -0.0324 S33:   -0.0442                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -37.5110  -48.4995  -42.7702           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0845 T22:    0.0282                                    
REMARK   3     T33:    0.0181 T12:   -0.1999                                    
REMARK   3     T13:   -0.1419 T23:   -0.0814                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.0115 L22:    0.2454                                    
REMARK   3     L33:   -0.2528 L12:    1.8918                                    
REMARK   3     L13:    1.2326 L23:    1.1555                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0035 S12:    0.0236 S13:   -0.0087                     
REMARK   3     S21:   -0.0186 S22:   -0.0121 S23:    0.0165                     
REMARK   3     S31:    0.0141 S32:   -0.0158 S33:    0.0156                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -14.8553    4.2530  -22.6720           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1144 T22:    0.1246                                    
REMARK   3     T33:   -0.0551 T12:    0.0468                                    
REMARK   3     T13:    0.0538 T23:   -0.0226                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.7614 L22:    0.0415                                    
REMARK   3     L33:    1.0108 L12:   -0.6507                                    
REMARK   3     L13:   -1.3075 L23:    0.3009                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0034 S12:   -0.0137 S13:    0.0172                     
REMARK   3     S21:    0.0546 S22:   -0.0263 S23:   -0.0062                     
REMARK   3     S31:   -0.0245 S32:   -0.0687 S33:    0.0229                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A):    5.1677    3.1355  -40.6802           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.1102 T22:   -0.0040                                    
REMARK   3     T33:   -0.0634 T12:    0.0381                                    
REMARK   3     T13:   -0.0027 T23:    0.0240                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.2236 L22:    1.3624                                    
REMARK   3     L33:    2.4182 L12:    0.5434                                    
REMARK   3     L13:   -0.7068 L23:   -0.1431                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0274 S12:   -0.0044 S13:    0.0391                     
REMARK   3     S21:   -0.0558 S22:    0.0412 S23:   -0.0165                     
REMARK   3     S31:   -0.0997 S32:    0.0891 S33:   -0.0138                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: NULL                                                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -28.4658   -2.0591  -34.0780           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0765 T22:    0.0951                                    
REMARK   3     T33:   -0.0234 T12:    0.0228                                    
REMARK   3     T13:   -0.0400 T23:   -0.0545                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.8767 L22:    0.0651                                    
REMARK   3     L33:   -0.1093 L12:   -0.1116                                    
REMARK   3     L13:    0.6993 L23:    0.2259                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0007 S12:   -0.0039 S13:    0.0026                     
REMARK   3     S21:   -0.0123 S22:   -0.0020 S23:    0.0027                     
REMARK   3     S31:    0.0053 S32:   -0.0070 S33:    0.0028                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4UMP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-MAY-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290060707.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-MAY-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E                        
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NI FILTER                          
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU IMAGE PLATE RAXIS           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 61286                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.800                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY                : 1.950                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.7000                             
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   (%): 46.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.7 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2660 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.9 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C                                  
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     LEU A    47                                                      
REMARK 465     GLY A    48                                                      
REMARK 465     SER A    49                                                      
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     ALA A   167                                                      
REMARK 465     CYS A   168                                                      
REMARK 465     CYS A   169                                                      
REMARK 465     SER A   184                                                      
REMARK 465     TYR A   185                                                      
REMARK 465     LEU A   186                                                      
REMARK 465     LEU A   334                                                      
REMARK 465     SER A   335                                                      
REMARK 465     SER A   336                                                      
REMARK 465     MET B   -19                                                      
REMARK 465     GLY B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     TYR B   163                                                      
REMARK 465     HIS B   164                                                      
REMARK 465     LEU B   165                                                      
REMARK 465     GLN B   166                                                      
REMARK 465     ALA B   167                                                      
REMARK 465     CYS B   168                                                      
REMARK 465     SER B   184                                                      
REMARK 465     TYR B   185                                                      
REMARK 465     LEU B   186                                                      
REMARK 465     LEU B   334                                                      
REMARK 465     SER B   335                                                      
REMARK 465     SER B   336                                                      
REMARK 465     MET C   -19                                                      
REMARK 465     GLY C   -18                                                      
REMARK 465     SER C   -17                                                      
REMARK 465     SER C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     HIS C   -10                                                      
REMARK 465     SER C    -9                                                      
REMARK 465     SER C    -8                                                      
REMARK 465     GLY C    -7                                                      
REMARK 465     LEU C    -6                                                      
REMARK 465     VAL C    -5                                                      
REMARK 465     PRO C    -4                                                      
REMARK 465     ARG C    -3                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     GLY C    20                                                      
REMARK 465     GLY C    21                                                      
REMARK 465     PHE C    22                                                      
REMARK 465     THR C    46                                                      
REMARK 465     LEU C    47                                                      
REMARK 465     GLY C    48                                                      
REMARK 465     PRO C   157                                                      
REMARK 465     LYS C   158                                                      
REMARK 465     GLY C   159                                                      
REMARK 465     ASN C   160                                                      
REMARK 465     LYS C   161                                                      
REMARK 465     ASP C   162                                                      
REMARK 465     TYR C   163                                                      
REMARK 465     HIS C   164                                                      
REMARK 465     LEU C   165                                                      
REMARK 465     GLN C   166                                                      
REMARK 465     ALA C   167                                                      
REMARK 465     CYS C   168                                                      
REMARK 465     CYS C   169                                                      
REMARK 465     SER C   184                                                      
REMARK 465     TYR C   185                                                      
REMARK 465     LEU C   186                                                      
REMARK 465     LEU C   334                                                      
REMARK 465     SER C   335                                                      
REMARK 465     SER C   336                                                      
REMARK 465     MET D   -19                                                      
REMARK 465     GLY D   -18                                                      
REMARK 465     SER D   -17                                                      
REMARK 465     SER D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     HIS D   -10                                                      
REMARK 465     SER D    -9                                                      
REMARK 465     SER D    -8                                                      
REMARK 465     GLY D    -7                                                      
REMARK 465     LEU D    -6                                                      
REMARK 465     VAL D    -5                                                      
REMARK 465     PRO D    -4                                                      
REMARK 465     ARG D    -3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     TYR D   163                                                      
REMARK 465     HIS D   164                                                      
REMARK 465     LEU D   165                                                      
REMARK 465     GLN D   166                                                      
REMARK 465     ALA D   167                                                      
REMARK 465     CYS D   168                                                      
REMARK 465     CYS D   169                                                      
REMARK 465     MET D   301                                                      
REMARK 465     GLU D   302                                                      
REMARK 465     ASP D   303                                                      
REMARK 465     LEU D   304                                                      
REMARK 465     LEU D   334                                                      
REMARK 465     SER D   335                                                      
REMARK 465     SER D   336                                                      
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     ASP A 102    CG   OD1  OD2                                       
REMARK 470     PHE B  22    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS C   2    CG   CD   CE   NZ                                   
REMARK 470     PHE D  22    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     HIS D 281    CG   ND1  CD2  CE1  NE2                             
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     -152.55   -113.28                                   
REMARK 500    PHE A  22      -11.53     70.88                                   
REMARK 500    THR A  78     -151.88   -116.24                                   
REMARK 500    ARG A 131       16.14     59.29                                   
REMARK 500    ASP A 132       37.76   -154.56                                   
REMARK 500    ASP A 150       81.11     54.54                                   
REMARK 500    LEU A 244       41.97    -99.34                                   
REMARK 500    ASN A 268       48.28    -86.55                                   
REMARK 500    ILE A 280      -60.63    -95.99                                   
REMARK 500    GLN A 299      -29.72     74.58                                   
REMARK 500    TRP A 308       62.83     39.58                                   
REMARK 500    ASP A 311     -169.98   -110.82                                   
REMARK 500    LYS B   2      -48.81     70.05                                   
REMARK 500    HIS B  14     -155.69   -113.94                                   
REMARK 500    PHE B  22      -17.26     63.53                                   
REMARK 500    ARG B  65      105.83   -163.49                                   
REMARK 500    THR B  78     -151.30   -114.81                                   
REMARK 500    ARG B 103      127.53    -30.47                                   
REMARK 500    ARG B 131       -5.05     71.20                                   
REMARK 500    ASP B 132       38.06   -140.67                                   
REMARK 500    ASP B 150       86.00     56.20                                   
REMARK 500    GLN B 181     -164.59    -78.52                                   
REMARK 500    LEU B 244       41.35    -98.19                                   
REMARK 500    ASP B 266      -19.92     71.98                                   
REMARK 500    ILE B 280      -65.36    -96.97                                   
REMARK 500    TRP B 308       61.98     39.48                                   
REMARK 500    HIS C  14     -152.04   -112.78                                   
REMARK 500    THR C  78     -151.20   -117.78                                   
REMARK 500    ARG C 131      -10.70     70.39                                   
REMARK 500    ASP C 141     -157.51    -74.53                                   
REMARK 500    ASP C 150       85.45     56.39                                   
REMARK 500    LEU C 244       43.04    -98.47                                   
REMARK 500    ASP C 266      -40.73   -140.58                                   
REMARK 500    ASN C 268       42.23    -75.87                                   
REMARK 500    ILE C 280      -62.13    -98.83                                   
REMARK 500    TRP C 308       63.40     37.72                                   
REMARK 500    ASP D   3      -19.27    101.01                                   
REMARK 500    HIS D  14     -154.80   -112.88                                   
REMARK 500    PHE D  22       48.03   -156.57                                   
REMARK 500    THR D  78     -151.31   -113.52                                   
REMARK 500    ASP D 102     -174.65    -65.31                                   
REMARK 500    ARG D 103      158.03    -48.99                                   
REMARK 500    ARG D 131       -6.44     69.30                                   
REMARK 500    HIS D 144       38.22     75.99                                   
REMARK 500    ASP D 150       81.99     60.45                                   
REMARK 500    LEU D 244       42.77    -97.28                                   
REMARK 500    ASP D 266      -39.58     79.63                                   
REMARK 500    ILE D 280      -61.82   -101.36                                   
REMARK 500    ARG D 295       79.57    -68.01                                   
REMARK 500    TRP D 308       63.31     39.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY C   18     THR C   19                 -116.27                    
REMARK 500 ASP D  283     ASP D  284                 -149.06                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A2057        DISTANCE =  6.32 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5QM D 1334                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5QM A 1334                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5QM B 1334                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5QM C 1334                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4D2T   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF MELK IN COMPLEX WITH INHIBITORS                         
REMARK 900 RELATED ID: 4D2V   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF MELK IN COMPLEX WITH INHIBITORS                         
REMARK 900 RELATED ID: 4D2W   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: 4UMT   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 EXIST IN THE SEQUENCE, IN ADDITION TO THE            
REMARK 999 HIS TAG                                                              
DBREF  4UMP A    1   336  UNP    Q14680   MELK_HUMAN       1    336             
DBREF  4UMP B    1   336  UNP    Q14680   MELK_HUMAN       1    336             
DBREF  4UMP C    1   336  UNP    Q14680   MELK_HUMAN       1    336             
DBREF  4UMP D    1   336  UNP    Q14680   MELK_HUMAN       1    336             
SEQADV 4UMP MET A  -19  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP GLY A  -18  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP SER A  -17  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP SER A  -16  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS A  -15  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS A  -14  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS A  -13  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS A  -12  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS A  -11  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS A  -10  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP SER A   -9  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP SER A   -8  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP GLY A   -7  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP LEU A   -6  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP VAL A   -5  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP PRO A   -4  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP ARG A   -3  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP GLY A   -2  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP SER A   -1  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS A    0  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP ALA A  167  UNP  Q14680    THR   167 ENGINEERED MUTATION            
SEQADV 4UMP ALA A  171  UNP  Q14680    SER   171 ENGINEERED MUTATION            
SEQADV 4UMP THR A  213  UNP  Q14680    ASN   213 ENGINEERED MUTATION            
SEQADV 4UMP ALA A  214  UNP  Q14680    VAL   214 ENGINEERED MUTATION            
SEQADV 4UMP ALA A  215  UNP  Q14680    MET   215 ENGINEERED MUTATION            
SEQADV 4UMP VAL A  218  UNP  Q14680    TYR   218 ENGINEERED MUTATION            
SEQADV 4UMP ALA A  219  UNP  Q14680    LYS   219 ENGINEERED MUTATION            
SEQADV 4UMP MET B  -19  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP GLY B  -18  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP SER B  -17  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP SER B  -16  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS B  -15  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS B  -14  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS B  -13  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS B  -12  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS B  -11  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS B  -10  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP SER B   -9  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP SER B   -8  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP GLY B   -7  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP LEU B   -6  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP VAL B   -5  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP PRO B   -4  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP ARG B   -3  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP GLY B   -2  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP SER B   -1  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS B    0  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP ALA B  167  UNP  Q14680    THR   167 ENGINEERED MUTATION            
SEQADV 4UMP ALA B  171  UNP  Q14680    SER   171 ENGINEERED MUTATION            
SEQADV 4UMP THR B  213  UNP  Q14680    ASN   213 ENGINEERED MUTATION            
SEQADV 4UMP ALA B  214  UNP  Q14680    VAL   214 ENGINEERED MUTATION            
SEQADV 4UMP ALA B  215  UNP  Q14680    MET   215 ENGINEERED MUTATION            
SEQADV 4UMP VAL B  218  UNP  Q14680    TYR   218 ENGINEERED MUTATION            
SEQADV 4UMP ALA B  219  UNP  Q14680    LYS   219 ENGINEERED MUTATION            
SEQADV 4UMP MET C  -19  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP GLY C  -18  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP SER C  -17  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP SER C  -16  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS C  -15  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS C  -14  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS C  -13  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS C  -12  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS C  -11  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS C  -10  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP SER C   -9  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP SER C   -8  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP GLY C   -7  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP LEU C   -6  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP VAL C   -5  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP PRO C   -4  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP ARG C   -3  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP GLY C   -2  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP SER C   -1  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS C    0  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP ALA C  167  UNP  Q14680    THR   167 ENGINEERED MUTATION            
SEQADV 4UMP ALA C  171  UNP  Q14680    SER   171 ENGINEERED MUTATION            
SEQADV 4UMP THR C  213  UNP  Q14680    ASN   213 ENGINEERED MUTATION            
SEQADV 4UMP ALA C  214  UNP  Q14680    VAL   214 ENGINEERED MUTATION            
SEQADV 4UMP ALA C  215  UNP  Q14680    MET   215 ENGINEERED MUTATION            
SEQADV 4UMP VAL C  218  UNP  Q14680    TYR   218 ENGINEERED MUTATION            
SEQADV 4UMP ALA C  219  UNP  Q14680    LYS   219 ENGINEERED MUTATION            
SEQADV 4UMP MET D  -19  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP GLY D  -18  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP SER D  -17  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP SER D  -16  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS D  -15  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS D  -14  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS D  -13  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS D  -12  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS D  -11  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS D  -10  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP SER D   -9  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP SER D   -8  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP GLY D   -7  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP LEU D   -6  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP VAL D   -5  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP PRO D   -4  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP ARG D   -3  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP GLY D   -2  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP SER D   -1  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP HIS D    0  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4UMP ALA D  167  UNP  Q14680    THR   167 ENGINEERED MUTATION            
SEQADV 4UMP ALA D  171  UNP  Q14680    SER   171 ENGINEERED MUTATION            
SEQADV 4UMP THR D  213  UNP  Q14680    ASN   213 ENGINEERED MUTATION            
SEQADV 4UMP ALA D  214  UNP  Q14680    VAL   214 ENGINEERED MUTATION            
SEQADV 4UMP ALA D  215  UNP  Q14680    MET   215 ENGINEERED MUTATION            
SEQADV 4UMP VAL D  218  UNP  Q14680    TYR   218 ENGINEERED MUTATION            
SEQADV 4UMP ALA D  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 ALA CYS CYS GLY ALA 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                                          
SEQRES   1 B  356  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  356  LEU VAL PRO ARG GLY SER HIS MET LYS ASP TYR ASP GLU          
SEQRES   3 B  356  LEU LEU LYS TYR TYR GLU LEU HIS GLU THR ILE GLY THR          
SEQRES   4 B  356  GLY GLY PHE ALA LYS VAL LYS LEU ALA CYS HIS ILE LEU          
SEQRES   5 B  356  THR GLY GLU MET VAL ALA ILE LYS ILE MET ASP LYS ASN          
SEQRES   6 B  356  THR LEU GLY SER ASP LEU PRO ARG ILE LYS THR GLU ILE          
SEQRES   7 B  356  GLU ALA LEU LYS ASN LEU ARG HIS GLN HIS ILE CYS GLN          
SEQRES   8 B  356  LEU TYR HIS VAL LEU GLU THR ALA ASN LYS ILE PHE MET          
SEQRES   9 B  356  VAL LEU GLU TYR CYS PRO GLY GLY GLU LEU PHE ASP TYR          
SEQRES  10 B  356  ILE ILE SER GLN ASP ARG LEU SER GLU GLU GLU THR ARG          
SEQRES  11 B  356  VAL VAL PHE ARG GLN ILE VAL SER ALA VAL ALA TYR VAL          
SEQRES  12 B  356  HIS SER GLN GLY TYR ALA HIS ARG ASP LEU LYS PRO GLU          
SEQRES  13 B  356  ASN LEU LEU PHE ASP GLU TYR HIS LYS LEU LYS LEU ILE          
SEQRES  14 B  356  ASP PHE GLY LEU CYS ALA LYS PRO LYS GLY ASN LYS ASP          
SEQRES  15 B  356  TYR HIS LEU GLN ALA CYS CYS GLY ALA LEU ALA TYR ALA          
SEQRES  16 B  356  ALA PRO GLU LEU ILE GLN GLY LYS SER TYR LEU GLY SER          
SEQRES  17 B  356  GLU ALA ASP VAL TRP SER MET GLY ILE LEU LEU TYR VAL          
SEQRES  18 B  356  LEU MET CYS GLY PHE LEU PRO PHE ASP ASP ASP THR ALA          
SEQRES  19 B  356  ALA ALA LEU VAL ALA LYS ILE MET ARG GLY LYS TYR ASP          
SEQRES  20 B  356  VAL PRO LYS TRP LEU SER PRO SER SER ILE LEU LEU LEU          
SEQRES  21 B  356  GLN GLN MET LEU GLN VAL ASP PRO LYS LYS ARG ILE SER          
SEQRES  22 B  356  MET LYS ASN LEU LEU ASN HIS PRO TRP ILE MET GLN ASP          
SEQRES  23 B  356  TYR ASN TYR PRO VAL GLU TRP GLN SER LYS ASN PRO PHE          
SEQRES  24 B  356  ILE HIS LEU ASP ASP ASP CYS VAL THR GLU LEU SER VAL          
SEQRES  25 B  356  HIS HIS ARG ASN ASN ARG GLN THR MET GLU ASP LEU ILE          
SEQRES  26 B  356  SER LEU TRP GLN TYR ASP HIS LEU THR ALA THR TYR LEU          
SEQRES  27 B  356  LEU LEU LEU ALA LYS LYS ALA ARG GLY LYS PRO VAL ARG          
SEQRES  28 B  356  LEU ARG LEU SER SER                                          
SEQRES   1 C  356  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  356  LEU VAL PRO ARG GLY SER HIS MET LYS ASP TYR ASP GLU          
SEQRES   3 C  356  LEU LEU LYS TYR TYR GLU LEU HIS GLU THR ILE GLY THR          
SEQRES   4 C  356  GLY GLY PHE ALA LYS VAL LYS LEU ALA CYS HIS ILE LEU          
SEQRES   5 C  356  THR GLY GLU MET VAL ALA ILE LYS ILE MET ASP LYS ASN          
SEQRES   6 C  356  THR LEU GLY SER ASP LEU PRO ARG ILE LYS THR GLU ILE          
SEQRES   7 C  356  GLU ALA LEU LYS ASN LEU ARG HIS GLN HIS ILE CYS GLN          
SEQRES   8 C  356  LEU TYR HIS VAL LEU GLU THR ALA ASN LYS ILE PHE MET          
SEQRES   9 C  356  VAL LEU GLU TYR CYS PRO GLY GLY GLU LEU PHE ASP TYR          
SEQRES  10 C  356  ILE ILE SER GLN ASP ARG LEU SER GLU GLU GLU THR ARG          
SEQRES  11 C  356  VAL VAL PHE ARG GLN ILE VAL SER ALA VAL ALA TYR VAL          
SEQRES  12 C  356  HIS SER GLN GLY TYR ALA HIS ARG ASP LEU LYS PRO GLU          
SEQRES  13 C  356  ASN LEU LEU PHE ASP GLU TYR HIS LYS LEU LYS LEU ILE          
SEQRES  14 C  356  ASP PHE GLY LEU CYS ALA LYS PRO LYS GLY ASN LYS ASP          
SEQRES  15 C  356  TYR HIS LEU GLN ALA CYS CYS GLY ALA LEU ALA TYR ALA          
SEQRES  16 C  356  ALA PRO GLU LEU ILE GLN GLY LYS SER TYR LEU GLY SER          
SEQRES  17 C  356  GLU ALA ASP VAL TRP SER MET GLY ILE LEU LEU TYR VAL          
SEQRES  18 C  356  LEU MET CYS GLY PHE LEU PRO PHE ASP ASP ASP THR ALA          
SEQRES  19 C  356  ALA ALA LEU VAL ALA LYS ILE MET ARG GLY LYS TYR ASP          
SEQRES  20 C  356  VAL PRO LYS TRP LEU SER PRO SER SER ILE LEU LEU LEU          
SEQRES  21 C  356  GLN GLN MET LEU GLN VAL ASP PRO LYS LYS ARG ILE SER          
SEQRES  22 C  356  MET LYS ASN LEU LEU ASN HIS PRO TRP ILE MET GLN ASP          
SEQRES  23 C  356  TYR ASN TYR PRO VAL GLU TRP GLN SER LYS ASN PRO PHE          
SEQRES  24 C  356  ILE HIS LEU ASP ASP ASP CYS VAL THR GLU LEU SER VAL          
SEQRES  25 C  356  HIS HIS ARG ASN ASN ARG GLN THR MET GLU ASP LEU ILE          
SEQRES  26 C  356  SER LEU TRP GLN TYR ASP HIS LEU THR ALA THR TYR LEU          
SEQRES  27 C  356  LEU LEU LEU ALA LYS LYS ALA ARG GLY LYS PRO VAL ARG          
SEQRES  28 C  356  LEU ARG LEU SER SER                                          
SEQRES   1 D  356  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  356  LEU VAL PRO ARG GLY SER HIS MET LYS ASP TYR ASP GLU          
SEQRES   3 D  356  LEU LEU LYS TYR TYR GLU LEU HIS GLU THR ILE GLY THR          
SEQRES   4 D  356  GLY GLY PHE ALA LYS VAL LYS LEU ALA CYS HIS ILE LEU          
SEQRES   5 D  356  THR GLY GLU MET VAL ALA ILE LYS ILE MET ASP LYS ASN          
SEQRES   6 D  356  THR LEU GLY SER ASP LEU PRO ARG ILE LYS THR GLU ILE          
SEQRES   7 D  356  GLU ALA LEU LYS ASN LEU ARG HIS GLN HIS ILE CYS GLN          
SEQRES   8 D  356  LEU TYR HIS VAL LEU GLU THR ALA ASN LYS ILE PHE MET          
SEQRES   9 D  356  VAL LEU GLU TYR CYS PRO GLY GLY GLU LEU PHE ASP TYR          
SEQRES  10 D  356  ILE ILE SER GLN ASP ARG LEU SER GLU GLU GLU THR ARG          
SEQRES  11 D  356  VAL VAL PHE ARG GLN ILE VAL SER ALA VAL ALA TYR VAL          
SEQRES  12 D  356  HIS SER GLN GLY TYR ALA HIS ARG ASP LEU LYS PRO GLU          
SEQRES  13 D  356  ASN LEU LEU PHE ASP GLU TYR HIS LYS LEU LYS LEU ILE          
SEQRES  14 D  356  ASP PHE GLY LEU CYS ALA LYS PRO LYS GLY ASN LYS ASP          
SEQRES  15 D  356  TYR HIS LEU GLN ALA CYS CYS GLY ALA LEU ALA TYR ALA          
SEQRES  16 D  356  ALA PRO GLU LEU ILE GLN GLY LYS SER TYR LEU GLY SER          
SEQRES  17 D  356  GLU ALA ASP VAL TRP SER MET GLY ILE LEU LEU TYR VAL          
SEQRES  18 D  356  LEU MET CYS GLY PHE LEU PRO PHE ASP ASP ASP THR ALA          
SEQRES  19 D  356  ALA ALA LEU VAL ALA LYS ILE MET ARG GLY LYS TYR ASP          
SEQRES  20 D  356  VAL PRO LYS TRP LEU SER PRO SER SER ILE LEU LEU LEU          
SEQRES  21 D  356  GLN GLN MET LEU GLN VAL ASP PRO LYS LYS ARG ILE SER          
SEQRES  22 D  356  MET LYS ASN LEU LEU ASN HIS PRO TRP ILE MET GLN ASP          
SEQRES  23 D  356  TYR ASN TYR PRO VAL GLU TRP GLN SER LYS ASN PRO PHE          
SEQRES  24 D  356  ILE HIS LEU ASP ASP ASP CYS VAL THR GLU LEU SER VAL          
SEQRES  25 D  356  HIS HIS ARG ASN ASN ARG GLN THR MET GLU ASP LEU ILE          
SEQRES  26 D  356  SER LEU TRP GLN TYR ASP HIS LEU THR ALA THR TYR LEU          
SEQRES  27 D  356  LEU LEU LEU ALA LYS LYS ALA ARG GLY LYS PRO VAL ARG          
SEQRES  28 D  356  LEU ARG LEU SER SER                                          
HET    5QM  A1334      23                                                       
HET    5QM  B1334      23                                                       
HET    5QM  C1334      23                                                       
HET    5QM  D1334      23                                                       
HETNAM     5QM 3-(ISOQUINOLIN-7-YL)PROP-2-YN-1-OL                               
FORMUL   5  5QM    4(C12 H9 N O)                                                
FORMUL   9  HOH   *564(H2 O)                                                    
HELIX    1   1 MET A    1  ASP A    5  5                                   5    
HELIX    2   2 GLU A    6  TYR A   10  1                                   5    
HELIX    3   3 ASP A   50  LEU A   64  1                                  15    
HELIX    4   4 GLU A   93  GLN A  101  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 ALA A  171  ALA A  175  5                                   5    
HELIX    8   8 ALA A  176  GLY A  182  1                                   7    
HELIX    9   9 SER A  188  GLY A  205  1                                  18    
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 SER A  253  ASN A  259  1                                   7    
HELIX   13  13 HIS A  260  GLN A  265  1                                   6    
HELIX   14  14 ASP A  283  ARG A  295  1                                  13    
HELIX   15  15 THR A  300  LEU A  307  1                                   8    
HELIX   16  16 ASP A  311  ARG A  326  1                                  16    
HELIX   17  17 GLU B    6  TYR B   10  1                                   5    
HELIX   18  18 LEU B   47  SER B   49  5                                   3    
HELIX   19  19 ASP B   50  LEU B   64  1                                  15    
HELIX   20  20 GLU B   93  SER B  100  1                                   8    
HELIX   21  21 SER B  105  GLN B  126  1                                  22    
HELIX   22  22 ALA B  171  ALA B  175  5                                   5    
HELIX   23  23 ALA B  176  GLN B  181  1                                   6    
HELIX   24  24 SER B  188  GLY B  205  1                                  18    
HELIX   25  25 THR B  213  GLY B  224  1                                  12    
HELIX   26  26 SER B  233  LEU B  244  1                                  12    
HELIX   27  27 SER B  253  ASN B  259  1                                   7    
HELIX   28  28 HIS B  260  GLN B  265  1                                   6    
HELIX   29  29 ASP B  283  ARG B  295  1                                  13    
HELIX   30  30 ASN B  297  SER B  306  1                                  10    
HELIX   31  31 ASP B  311  GLY B  327  1                                  17    
HELIX   32  32 GLU C    6  TYR C   10  1                                   5    
HELIX   33  33 ASP C   50  LEU C   64  1                                  15    
HELIX   34  34 GLU C   93  GLN C  101  1                                   9    
HELIX   35  35 SER C  105  GLN C  126  1                                  22    
HELIX   36  36 ALA C  171  ALA C  175  5                                   5    
HELIX   37  37 ALA C  176  GLY C  182  1                                   7    
HELIX   38  38 SER C  188  GLY C  205  1                                  18    
HELIX   39  39 THR C  213  GLY C  224  1                                  12    
HELIX   40  40 SER C  233  LEU C  244  1                                  12    
HELIX   41  41 SER C  253  ASN C  259  1                                   7    
HELIX   42  42 ASP C  283  HIS C  294  1                                  12    
HELIX   43  43 ASN C  297  SER C  306  1                                  10    
HELIX   44  44 ASP C  311  GLY C  327  1                                  17    
HELIX   45  45 GLU D    6  TYR D   10  1                                   5    
HELIX   46  46 LYS D   44  GLY D   48  1                                   5    
HELIX   47  47 ASP D   50  LEU D   64  1                                  15    
HELIX   48  48 GLU D   93  GLN D  101  1                                   9    
HELIX   49  49 SER D  105  GLN D  126  1                                  22    
HELIX   50  50 ALA D  171  ALA D  175  5                                   5    
HELIX   51  51 ALA D  176  GLY D  182  1                                   7    
HELIX   52  52 SER D  188  GLY D  205  1                                  18    
HELIX   53  53 THR D  213  GLY D  224  1                                  12    
HELIX   54  54 SER D  233  LEU D  244  1                                  12    
HELIX   55  55 SER D  253  ASN D  259  1                                   7    
HELIX   56  56 HIS D  260  GLN D  265  1                                   6    
HELIX   57  57 ASP D  284  HIS D  294  1                                  11    
HELIX   58  58 ASP D  311  ARG D  326  1                                  16    
SHEET    1  AA 5 TYR A  11  GLY A  20  0                                        
SHEET    2  AA 5 ALA A  23  HIS A  30 -1  O  ALA A  23   N  GLY A  20           
SHEET    3  AA 5 MET A  36  ASP A  43 -1  O  VAL A  37   N  ALA A  28           
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 2 LEU A 138  PHE A 140  0                                        
SHEET    2  AB 2 LEU A 146  LEU A 148 -1  O  LYS A 147   N  LEU A 139           
SHEET    1  BA 5 TYR B  11  THR B  19  0                                        
SHEET    2  BA 5 LYS B  24  HIS B  30 -1  O  VAL B  25   N  ILE B  17           
SHEET    3  BA 5 MET B  36  ASP B  43 -1  O  VAL B  37   N  ALA B  28           
SHEET    4  BA 5 LYS B  81  GLU B  87 -1  O  ILE B  82   N  MET B  42           
SHEET    5  BA 5 LEU B  72  GLU B  77 -1  N  TYR B  73   O  VAL B  85           
SHEET    1  BB 2 LEU B 138  PHE B 140  0                                        
SHEET    2  BB 2 LEU B 146  LEU B 148 -1  O  LYS B 147   N  LEU B 139           
SHEET    1  CA 5 TYR C  11  GLY C  18  0                                        
SHEET    2  CA 5 LYS C  24  HIS C  30 -1  O  VAL C  25   N  ILE C  17           
SHEET    3  CA 5 MET C  36  ASP C  43 -1  O  VAL C  37   N  ALA C  28           
SHEET    4  CA 5 LYS C  81  GLU C  87 -1  O  ILE C  82   N  MET C  42           
SHEET    5  CA 5 LEU C  72  GLU C  77 -1  N  TYR C  73   O  VAL C  85           
SHEET    1  CB 2 LEU C 138  PHE C 140  0                                        
SHEET    2  CB 2 LEU C 146  LEU C 148 -1  O  LYS C 147   N  LEU C 139           
SHEET    1  DA 5 TYR D  11  THR D  19  0                                        
SHEET    2  DA 5 LYS D  24  HIS D  30 -1  O  VAL D  25   N  ILE D  17           
SHEET    3  DA 5 MET D  36  ASP D  43 -1  O  VAL D  37   N  ALA D  28           
SHEET    4  DA 5 LYS D  81  GLU D  87 -1  O  ILE D  82   N  MET D  42           
SHEET    5  DA 5 LEU D  72  GLU D  77 -1  N  TYR D  73   O  VAL D  85           
SHEET    1  DB 2 LEU D 138  PHE D 140  0                                        
SHEET    2  DB 2 LEU D 146  LEU D 148 -1  O  LYS D 147   N  LEU D 139           
SITE     1 AC1  8 ALA D  38  GLU D  57  GLU D  87  CYS D  89                    
SITE     2 AC1  8 LEU D 139  ILE D 149  ASP D 150  HOH D2034                    
SITE     1 AC2  9 ILE A  17  ALA A  38  GLU A  57  GLU A  87                    
SITE     2 AC2  9 CYS A  89  LEU A 139  ILE A 149  ASP A 150                    
SITE     3 AC2  9 HOH A2043                                                     
SITE     1 AC3  8 ILE B  17  ALA B  38  GLU B  57  GLU B  87                    
SITE     2 AC3  8 CYS B  89  ILE B 149  ASP B 150  HOH B2043                    
SITE     1 AC4 10 ILE C  17  VAL C  25  ALA C  38  GLU C  57                    
SITE     2 AC4 10 GLU C  87  CYS C  89  LEU C 139  ILE C 149                    
SITE     3 AC4 10 ASP C 150  HOH C2036                                          
CRYST1   65.822   74.968   77.088  86.47  70.06  89.94 P 1           4          
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      0.015192 -0.000016 -0.005522        0.00000                         
SCALE2      0.000000  0.013339 -0.000870        0.00000                         
SCALE3      0.000000  0.000000  0.013829        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system