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Database: PDB
Entry: 4D2T
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HEADER    TRANSFERASE                             13-MAY-14   4D2T              
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 FRAGMENT: RESIDUES 1-336;                                            
COMPND   5 SYNONYM: HMELK, PROTEIN KINASE EG3, PEG3 KINASE, PROTEIN KINASE PK38,
COMPND   6 HPK38, TYROSINE-PROTEIN KINASE MELK, HMELK, PROTEIN KINASE EG3, PEG3 
COMPND   7 KINASE, PROTEIN KINASE PK38 , HPK38, TYROSINE-PROTEIN KINASE MELK,   
COMPND   8 MELK;                                                                
COMPND   9 EC: 2.7.11.1, 2.7.10.2;                                              
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 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, KINASE                       
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   4   04-APR-18 4D2T    1       REMARK ATOM                              
REVDAT   3   18-MAR-15 4D2T    1       REMARK                                   
REVDAT   2   28-JAN-15 4D2T    1       JRNL                                     
REVDAT   1   15-OCT-14 4D2T    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.    2.70 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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.54                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 36893                          
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)  : 0.273                          
REMARK   3   R VALUE            (WORKING SET)  : 0.270                          
REMARK   3   FREE R VALUE                      : 0.340                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.070                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1870                           
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               : 18                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.70                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.78                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 93.14                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2372                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2504                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2249                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2469                   
REMARK   3   BIN FREE R VALUE                        : 0.3179                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 5.19                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 123                      
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            : 10279                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 100                                     
REMARK   3   SOLVENT ATOMS            : 396                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 84.38                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 89.48                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 8.53370                                              
REMARK   3    B22 (A**2) : -2.62090                                             
REMARK   3    B33 (A**2) : -5.91280                                             
REMARK   3    B12 (A**2) : -1.96840                                             
REMARK   3    B13 (A**2) : -7.75930                                             
REMARK   3    B23 (A**2) : -0.63590                                             
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.674               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.491               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
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      : 0.915                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.856                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 10706  ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 14533  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 3741   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 253    ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 1550   ; 16.000 ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 10706  ; 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   : 1335   ; 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   : 11861  ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.11                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 6.00                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 22.59                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 12                                         
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND RESIDUES 1 TO 91                           
REMARK   3    ORIGIN FOR THE GROUP (A):    9.8447   -0.1651  -11.1599           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2119 T22:   -0.2333                                    
REMARK   3     T33:    0.1822 T12:    0.2117                                    
REMARK   3     T13:    0.2134 T23:    0.1212                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.6932 L22:    0.8161                                    
REMARK   3     L33:    5.3691 L12:   -0.0875                                    
REMARK   3     L13:   -3.6114 L23:    0.0813                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0607 S12:    0.4207 S13:    0.1113                     
REMARK   3     S21:   -0.3382 S22:   -0.0288 S23:   -0.4470                     
REMARK   3     S31:   -0.1360 S32:    0.2844 S33:    0.0895                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND RESIDUES 92 TO 274                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -10.7002    4.2767    6.6559           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0351 T22:   -0.3071                                    
REMARK   3     T33:   -0.0252 T12:    0.0906                                    
REMARK   3     T13:    0.1529 T23:   -0.0454                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.0387 L22:    7.3877                                    
REMARK   3     L33:    2.0750 L12:   -1.0016                                    
REMARK   3     L13:   -1.0738 L23:    0.7348                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0097 S12:   -0.0335 S13:    0.1727                     
REMARK   3     S21:    0.7120 S22:   -0.1086 S23:    0.3332                     
REMARK   3     S31:    0.0684 S32:   -0.1897 S33:    0.1183                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND RESIDUES 275 TO 333                        
REMARK   3    ORIGIN FOR THE GROUP (A):   20.4232  -11.3644    0.3483           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3229 T22:   -0.2518                                    
REMARK   3     T33:    0.3158 T12:    0.2000                                    
REMARK   3     T13:    0.0693 T23:    0.1274                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.1165 L22:    0.4112                                    
REMARK   3     L33:    4.1571 L12:   -3.8061                                    
REMARK   3     L13:   -1.5121 L23:   -1.4927                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0871 S12:    0.0210 S13:    0.0240                     
REMARK   3     S21:    0.1689 S22:   -0.1214 S23:   -0.1452                     
REMARK   3     S31:    0.2204 S32:    0.2618 S33:    0.0343                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN B AND RESIDUES 0 TO 91                           
REMARK   3    ORIGIN FOR THE GROUP (A):   -2.5330  -34.1549  -20.7370           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2580 T22:   -0.1319                                    
REMARK   3     T33:   -0.0360 T12:    0.0304                                    
REMARK   3     T13:    0.0754 T23:   -0.0086                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.0381 L22:    5.3384                                    
REMARK   3     L33:    6.4406 L12:   -0.5305                                    
REMARK   3     L13:   -2.8429 L23:   -1.3655                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0583 S12:    0.1982 S13:   -0.0584                     
REMARK   3     S21:   -0.7120 S22:   -0.0025 S23:   -0.2951                     
REMARK   3     S31:   -0.1837 S32:    0.1588 S33:    0.0608                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN B AND RESIDUES 92 TO 274                         
REMARK   3    ORIGIN FOR THE GROUP (A):  -22.6052  -35.1702   -2.0576           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2774 T22:   -0.2861                                    
REMARK   3     T33:    0.0622 T12:    0.1586                                    
REMARK   3     T13:    0.0837 T23:   -0.0018                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.1598 L22:    3.2647                                    
REMARK   3     L33:    5.6784 L12:    0.0197                                    
REMARK   3     L13:   -1.7444 L23:   -1.1623                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0197 S12:    0.3849 S13:    0.1177                     
REMARK   3     S21:    0.3213 S22:    0.2385 S23:    0.4200                     
REMARK   3     S31:   -0.3827 S32:   -0.4792 S33:   -0.2583                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN B AND RESIDUES 275 TO 333                        
REMARK   3    ORIGIN FOR THE GROUP (A):   11.4173  -39.2354   -8.2652           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3383 T22:    0.1257                                    
REMARK   3     T33:    0.2195 T12:   -0.0399                                    
REMARK   3     T13:    0.0557 T23:    0.1841                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.2901 L22:    0.1345                                    
REMARK   3     L33:    1.6903 L12:   -1.8283                                    
REMARK   3     L13:    3.3026 L23:   -0.3457                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0387 S12:   -0.1518 S13:   -0.0393                     
REMARK   3     S21:    0.1213 S22:   -0.1356 S23:   -0.0747                     
REMARK   3     S31:    0.0696 S32:    0.2369 S33:    0.0969                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN C AND RESIDUES 1 TO 91                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -28.0626  -37.9995  -32.6021           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3178 T22:   -0.3080                                    
REMARK   3     T33:    0.3361 T12:   -0.1906                                    
REMARK   3     T13:    0.1047 T23:   -0.0441                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    3.7361 L22:    1.5021                                    
REMARK   3     L33:    5.5646 L12:   -1.0372                                    
REMARK   3     L13:   -3.0002 L23:    0.3530                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1038 S12:   -0.3031 S13:   -0.1313                     
REMARK   3     S21:    0.1868 S22:    0.0536 S23:    0.4993                     
REMARK   3     S31:   -0.1519 S32:   -0.2420 S33:    0.0502                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN C AND RESIDUES 92 TO 274                         
REMARK   3    ORIGIN FOR THE GROUP (A):   -7.1326  -33.3072  -49.7337           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.1371 T22:   -0.3026                                    
REMARK   3     T33:   -0.0254 T12:    0.0185                                    
REMARK   3     T13:    0.1309 T23:    0.0180                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    6.5768 L22:    7.3419                                    
REMARK   3     L33:    1.0566 L12:    2.1537                                    
REMARK   3     L13:   -1.8400 L23:   -1.1808                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.1224 S12:    0.2157 S13:    0.5027                     
REMARK   3     S21:   -0.6849 S22:   -0.1571 S23:   -0.2746                     
REMARK   3     S31:    0.1154 S32:    0.2336 S33:    0.0348                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN C AND RESIDUES 275 TO 333                        
REMARK   3    ORIGIN FOR THE GROUP (A):  -38.4184  -48.8380  -44.2353           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0419 T22:   -0.3061                                    
REMARK   3     T33:    0.2731 T12:   -0.1935                                    
REMARK   3     T13:   -0.0479 T23:   -0.0522                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.6204 L22:    0.4009                                    
REMARK   3     L33:    0.8141 L12:    3.0894                                    
REMARK   3     L13:    0.1832 L23:    1.9221                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0483 S12:    0.1221 S13:    0.0935                     
REMARK   3     S21:   -0.0950 S22:   -0.1028 S23:    0.1427                     
REMARK   3     S31:    0.0807 S32:   -0.1605 S33:    0.0546                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN D AND RESIDUES 3 TO 91                           
REMARK   3    ORIGIN FOR THE GROUP (A):  -15.2961    3.7380  -22.9576           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2862 T22:   -0.1136                                    
REMARK   3     T33:   -0.0480 T12:    0.0152                                    
REMARK   3     T13:    0.0651 T23:   -0.0177                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    4.9058 L22:    4.9852                                    
REMARK   3     L33:    8.1765 L12:   -0.9560                                    
REMARK   3     L13:   -2.2914 L23:    2.3714                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0507 S12:   -0.6396 S13:   -0.0883                     
REMARK   3     S21:    0.6392 S22:    0.0227 S23:    0.1559                     
REMARK   3     S31:   -0.0610 S32:   -0.1729 S33:    0.0280                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN D AND RESIDUES 92 TO 274                         
REMARK   3    ORIGIN FOR THE GROUP (A):    4.3987    3.0440  -41.2053           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2771 T22:   -0.3189                                    
REMARK   3     T33:    0.0405 T12:   -0.0774                                    
REMARK   3     T13:    0.1010 T23:   -0.0710                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    5.9254 L22:    3.3719                                    
REMARK   3     L33:    7.0815 L12:   -0.3828                                    
REMARK   3     L13:   -3.3501 L23:    0.6651                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0327 S12:   -0.3330 S13:    0.3573                     
REMARK   3     S21:   -0.3723 S22:    0.1404 S23:   -0.4543                     
REMARK   3     S31:   -0.3960 S32:    0.5711 S33:   -0.1731                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN D AND RESIDUES 275 TO 333                        
REMARK   3    ORIGIN FOR THE GROUP (A):  -28.9288   -1.8508  -34.8958           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.3345 T22:    0.2831                                    
REMARK   3     T33:    0.2904 T12:    0.0122                                    
REMARK   3     T13:    0.0698 T23:   -0.1678                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.1261 L22:    1.3092                                    
REMARK   3     L33:    2.4631 L12:    3.2980                                    
REMARK   3     L13:    2.4643 L23:    0.3237                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0015 S12:    0.0373 S13:    0.0015                     
REMARK   3     S21:   -0.0349 S22:   -0.0868 S23:    0.2877                     
REMARK   3     S31:    0.0450 S32:   -0.4097 S33:    0.0883                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4D2T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-MAY-14.                  
REMARK 100 THE DEPOSITION ID IS D_1290060608.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-SEP-09                          
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                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN                      
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39601                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.750                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.1                               
REMARK 200  DATA REDUNDANCY                : 1.900                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.9000                             
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, 3, 4                                              
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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: 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 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
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: 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 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     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     PHE B    22                                                      
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     LYS B   183                                                      
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     ASN C    45                                                      
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     LYS D     2                                                      
REMARK 465     ASP D   162                                                      
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     ARG D   295                                                      
REMARK 465     ASN D   296                                                      
REMARK 465     ASN D   297                                                      
REMARK 465     ARG D   298                                                      
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     LYS A   9    CG   CD   CE   NZ                                   
REMARK 470     CYS A 168    SG                                                  
REMARK 470     SER A 184    OG                                                  
REMARK 470     LYS C   2    CG   CD   CE   NZ                                   
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    MET A   264     O    TYR A   267              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  23       16.53    -61.08                                   
REMARK 500    CYS A  89       76.68   -114.98                                   
REMARK 500    ASP A 102       70.16     64.36                                   
REMARK 500    ARG A 103      163.01     62.35                                   
REMARK 500    ASP A 132       43.41   -149.66                                   
REMARK 500    ASP A 150       75.10     57.39                                   
REMARK 500    VAL A 292        5.39    -69.07                                   
REMARK 500    ASN A 296     -156.48   -121.71                                   
REMARK 500    GLN A 299      -45.12     68.81                                   
REMARK 500    ASP A 311     -156.86   -105.92                                   
REMARK 500    HIS B  14     -146.75   -136.56                                   
REMARK 500    THR B  19     -101.73     94.75                                   
REMARK 500    CYS B  70      109.26    -57.10                                   
REMARK 500    CYS B  89       76.53   -115.09                                   
REMARK 500    ASP B 102      -71.39    -71.03                                   
REMARK 500    ASP B 132       43.21   -148.08                                   
REMARK 500    ASP B 150       74.90     55.46                                   
REMARK 500    ASP B 266      -11.07     84.66                                   
REMARK 500    ARG B 295       64.00     66.41                                   
REMARK 500    ASP B 311     -156.37   -106.75                                   
REMARK 500    VAL B 330       85.58    -63.31                                   
REMARK 500    HIS C  14     -159.01   -137.48                                   
REMARK 500    THR C  78     -135.46   -134.83                                   
REMARK 500    CYS C  89       76.78   -114.36                                   
REMARK 500    ASP C 132       42.31   -145.78                                   
REMARK 500    ASP C 150       74.82     57.66                                   
REMARK 500    LYS C 225       83.76     47.70                                   
REMARK 500    LEU C 244       59.29    -91.80                                   
REMARK 500    GLN C 265      -49.48    -23.70                                   
REMARK 500    TYR C 269      148.03    170.88                                   
REMARK 500    ARG C 295       24.61    107.49                                   
REMARK 500    ASN C 297     -151.48   -120.07                                   
REMARK 500    ASP C 311     -156.67   -106.00                                   
REMARK 500    VAL C 330       79.39    -62.61                                   
REMARK 500    THR D  19       88.18    -63.97                                   
REMARK 500    CYS D  89       74.27   -115.08                                   
REMARK 500    ASP D 132       42.52   -146.39                                   
REMARK 500    ASP D 150       83.30     58.81                                   
REMARK 500    LYS D 183      137.09     57.19                                   
REMARK 500    SER D 184       92.99    -57.08                                   
REMARK 500    LEU D 244       62.26   -100.16                                   
REMARK 500    ASP D 266      -24.17     82.04                                   
REMARK 500    HIS D 281      140.08    -34.92                                   
REMARK 500    LEU D 282      -55.00   -139.39                                   
REMARK 500    HIS D 293      -81.08    -81.82                                   
REMARK 500    GLU D 302      143.59    -23.94                                   
REMARK 500    ASP D 303       -5.54     75.56                                   
REMARK 500    LEU D 304      106.18     59.32                                   
REMARK 500    SER D 306       -4.08    -53.29                                   
REMARK 500    ASP D 311     -156.23   -106.55                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      51 RAMACHANDRAN OUTLIERS.                        
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 A2020        DISTANCE =  6.25 ANGSTROMS                       
REMARK 525    HOH B2034        DISTANCE =  6.51 ANGSTROMS                       
REMARK 525    HOH C2005        DISTANCE =  5.91 ANGSTROMS                       
REMARK 525    HOH C2020        DISTANCE =  6.58 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3I7 D 1334                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3I7 A 1334                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3I7 B 1334                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3I7 C 1334                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4D2P   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: 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 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 HIS TAG ADDED AND C-TERMINAL RESIDUES NOT INCLUDED (304)             
DBREF  4D2T A    1   336  UNP    Q14680   MELK_HUMAN       1    336             
DBREF  4D2T B    1   336  UNP    Q14680   MELK_HUMAN       1    336             
DBREF  4D2T C    1   336  UNP    Q14680   MELK_HUMAN       1    336             
DBREF  4D2T D    1   336  UNP    Q14680   MELK_HUMAN       1    336             
SEQADV 4D2T MET A  -19  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T GLY A  -18  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T SER A  -17  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T SER A  -16  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS A  -15  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS A  -14  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS A  -13  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS A  -12  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS A  -11  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS A  -10  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T SER A   -9  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T SER A   -8  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T GLY A   -7  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T LEU A   -6  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T VAL A   -5  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T PRO A   -4  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T ARG A   -3  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T GLY A   -2  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T SER A   -1  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS A    0  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T ALA A  167  UNP  Q14680    THR   167 ENGINEERED MUTATION            
SEQADV 4D2T ALA A  171  UNP  Q14680    SER   171 ENGINEERED MUTATION            
SEQADV 4D2T THR A  213  UNP  Q14680    ASN   213 ENGINEERED MUTATION            
SEQADV 4D2T ALA A  214  UNP  Q14680    VAL   214 ENGINEERED MUTATION            
SEQADV 4D2T ALA A  215  UNP  Q14680    MET   215 ENGINEERED MUTATION            
SEQADV 4D2T VAL A  218  UNP  Q14680    TYR   218 ENGINEERED MUTATION            
SEQADV 4D2T ALA A  219  UNP  Q14680    LYS   219 ENGINEERED MUTATION            
SEQADV 4D2T MET B  -19  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T GLY B  -18  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T SER B  -17  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T SER B  -16  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS B  -15  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS B  -14  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS B  -13  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS B  -12  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS B  -11  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS B  -10  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T SER B   -9  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T SER B   -8  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T GLY B   -7  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T LEU B   -6  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T VAL B   -5  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T PRO B   -4  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T ARG B   -3  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T GLY B   -2  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T SER B   -1  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS B    0  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T ALA B  167  UNP  Q14680    THR   167 ENGINEERED MUTATION            
SEQADV 4D2T ALA B  171  UNP  Q14680    SER   171 ENGINEERED MUTATION            
SEQADV 4D2T THR B  213  UNP  Q14680    ASN   213 ENGINEERED MUTATION            
SEQADV 4D2T ALA B  214  UNP  Q14680    VAL   214 ENGINEERED MUTATION            
SEQADV 4D2T ALA B  215  UNP  Q14680    MET   215 ENGINEERED MUTATION            
SEQADV 4D2T VAL B  218  UNP  Q14680    TYR   218 ENGINEERED MUTATION            
SEQADV 4D2T ALA B  219  UNP  Q14680    LYS   219 ENGINEERED MUTATION            
SEQADV 4D2T MET C  -19  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T GLY C  -18  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T SER C  -17  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T SER C  -16  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS C  -15  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS C  -14  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS C  -13  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS C  -12  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS C  -11  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS C  -10  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T SER C   -9  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T SER C   -8  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T GLY C   -7  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T LEU C   -6  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T VAL C   -5  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T PRO C   -4  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T ARG C   -3  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T GLY C   -2  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T SER C   -1  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS C    0  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T ALA C  167  UNP  Q14680    THR   167 ENGINEERED MUTATION            
SEQADV 4D2T ALA C  171  UNP  Q14680    SER   171 ENGINEERED MUTATION            
SEQADV 4D2T THR C  213  UNP  Q14680    ASN   213 ENGINEERED MUTATION            
SEQADV 4D2T ALA C  214  UNP  Q14680    VAL   214 ENGINEERED MUTATION            
SEQADV 4D2T ALA C  215  UNP  Q14680    MET   215 ENGINEERED MUTATION            
SEQADV 4D2T VAL C  218  UNP  Q14680    TYR   218 ENGINEERED MUTATION            
SEQADV 4D2T ALA C  219  UNP  Q14680    LYS   219 ENGINEERED MUTATION            
SEQADV 4D2T MET D  -19  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T GLY D  -18  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T SER D  -17  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T SER D  -16  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS D  -15  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS D  -14  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS D  -13  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS D  -12  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS D  -11  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS D  -10  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T SER D   -9  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T SER D   -8  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T GLY D   -7  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T LEU D   -6  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T VAL D   -5  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T PRO D   -4  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T ARG D   -3  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T GLY D   -2  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T SER D   -1  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T HIS D    0  UNP  Q14680              EXPRESSION TAG                 
SEQADV 4D2T ALA D  167  UNP  Q14680    THR   167 ENGINEERED MUTATION            
SEQADV 4D2T ALA D  171  UNP  Q14680    SER   171 ENGINEERED MUTATION            
SEQADV 4D2T THR D  213  UNP  Q14680    ASN   213 ENGINEERED MUTATION            
SEQADV 4D2T ALA D  214  UNP  Q14680    VAL   214 ENGINEERED MUTATION            
SEQADV 4D2T ALA D  215  UNP  Q14680    MET   215 ENGINEERED MUTATION            
SEQADV 4D2T VAL D  218  UNP  Q14680    TYR   218 ENGINEERED MUTATION            
SEQADV 4D2T 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    3I7  A1334      46                                                       
HET    3I7  B1334      46                                                       
HET    3I7  C1334      46                                                       
HET    3I7  D1334      46                                                       
HETNAM     3I7 3-[2-(PHENYLCARBAMOYL)-5-(1H-PYRAZOL-4-YL)                       
HETNAM   2 3I7  PHENOXY]PROPAN-1-AMINIUM                                        
FORMUL   5  3I7    4(C19 H21 N4 O2 1+)                                          
FORMUL   9  HOH   *396(H2 O)                                                    
HELIX    1   1 LEU A   51  LEU A   64  1                                  14    
HELIX    2   2 GLU A   93  ASP A  102  1                                  10    
HELIX    3   3 SER A  105  GLN A  126  1                                  22    
HELIX    4   4 ALA A  171  ALA A  175  5                                   5    
HELIX    5   5 ALA A  176  GLN A  181  1                                   6    
HELIX    6   6 SER A  188  GLY A  205  1                                  18    
HELIX    7   7 THR A  213  GLY A  224  1                                  12    
HELIX    8   8 SER A  233  LEU A  244  1                                  12    
HELIX    9   9 SER A  253  ASN A  259  1                                   7    
HELIX   10  10 HIS A  260  GLN A  265  1                                   6    
HELIX   11  11 ASP A  283  ARG A  295  1                                  13    
HELIX   12  12 MET A  301  SER A  306  1                                   6    
HELIX   13  13 ASP A  311  ARG A  326  1                                  16    
HELIX   14  14 ASP B   50  LYS B   62  1                                  13    
HELIX   15  15 GLU B   93  GLN B  101  1                                   9    
HELIX   16  16 SER B  105  GLN B  126  1                                  22    
HELIX   17  17 ALA B  171  ALA B  175  5                                   5    
HELIX   18  18 ALA B  176  GLN B  181  1                                   6    
HELIX   19  19 SER B  188  GLY B  205  1                                  18    
HELIX   20  20 THR B  213  GLY B  224  1                                  12    
HELIX   21  21 SER B  233  LEU B  244  1                                  12    
HELIX   22  22 SER B  253  ASN B  259  1                                   7    
HELIX   23  23 HIS B  260  GLN B  265  1                                   6    
HELIX   24  24 ASP B  283  ARG B  295  1                                  13    
HELIX   25  25 ASN B  297  SER B  306  1                                  10    
HELIX   26  26 ASP B  311  GLY B  327  1                                  17    
HELIX   27  27 MET C    1  ASP C    5  5                                   5    
HELIX   28  28 LEU C   51  LEU C   64  1                                  14    
HELIX   29  29 GLU C   93  GLN C  101  1                                   9    
HELIX   30  30 SER C  105  GLN C  126  1                                  22    
HELIX   31  31 ALA C  171  ALA C  175  5                                   5    
HELIX   32  32 ALA C  176  GLN C  181  1                                   6    
HELIX   33  33 SER C  188  GLY C  205  1                                  18    
HELIX   34  34 THR C  213  GLY C  224  1                                  12    
HELIX   35  35 SER C  233  LEU C  244  1                                  12    
HELIX   36  36 SER C  253  ASN C  259  1                                   7    
HELIX   37  37 HIS C  260  GLN C  265  1                                   6    
HELIX   38  38 CYS C  286  ARG C  295  1                                  10    
HELIX   39  39 MET C  301  SER C  306  1                                   6    
HELIX   40  40 ASP C  311  ALA C  325  1                                  15    
HELIX   41  41 LEU D   47  SER D   49  5                                   3    
HELIX   42  42 ASP D   50  LEU D   64  1                                  15    
HELIX   43  43 GLU D   93  GLN D  101  1                                   9    
HELIX   44  44 SER D  105  GLN D  126  1                                  22    
HELIX   45  45 ALA D  171  ALA D  175  5                                   5    
HELIX   46  46 ALA D  176  GLY D  182  1                                   7    
HELIX   47  47 SER D  188  GLY D  205  1                                  18    
HELIX   48  48 THR D  213  GLY D  224  1                                  12    
HELIX   49  49 SER D  233  LEU D  244  1                                  12    
HELIX   50  50 SER D  253  ASN D  259  1                                   7    
HELIX   51  51 HIS D  260  GLN D  265  1                                   6    
HELIX   52  52 ASP D  284  HIS D  293  1                                  10    
HELIX   53  53 ASP D  311  ARG D  326  1                                  16    
SHEET    1  AA 4 LYS A  24  CYS A  29  0                                        
SHEET    2  AA 4 MET A  36  ASP A  43 -1  O  VAL A  37   N  ALA A  28           
SHEET    3  AA 4 LYS A  81  GLU A  87 -1  O  ILE A  82   N  MET A  42           
SHEET    4  AA 4 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  16  0                                        
SHEET    2  BA 5 LYS B  24  HIS B  30 -1  O  LEU B  27   N  HIS B  14           
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  LEU C  13  0                                        
SHEET    2  CA 5 LYS C  24  HIS C  30 -1  O  CYS C  29   N  GLU C  12           
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  VAL C  75 -1  N  TYR C  73   O  VAL C  85           
SHEET    1  CB 2 LEU C 138  ASP C 141  0                                        
SHEET    2  CB 2 LYS C 145  LEU C 148 -1  O  LYS C 145   N  ASP C 141           
SHEET    1  DA 5 TYR D  11  THR D  16  0                                        
SHEET    2  DA 5 LYS D  24  HIS D  30 -1  O  LEU D  27   N  HIS D  14           
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  LEU D  76 -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           
CISPEP   1 GLU D  302    ASP D  303          0         1.38                     
SITE     1 AC1 10 ILE D  17  ALA D  38  GLU D  87  TYR D  88                    
SITE     2 AC1 10 CYS D  89  PRO D  90  GLY D  92  LEU D 139                    
SITE     3 AC1 10 ILE D 149  HOH D2021                                          
SITE     1 AC2 13 ALA A  23  VAL A  25  LEU A  27  ALA A  38                    
SITE     2 AC2 13 LYS A  40  GLU A  57  CYS A  70  GLU A  87                    
SITE     3 AC2 13 TYR A  88  CYS A  89  PRO A  90  ILE A 149                    
SITE     4 AC2 13 ASP A 150                                                     
SITE     1 AC3  8 ILE B  17  LEU B  27  ALA B  38  GLU B  87                    
SITE     2 AC3  8 CYS B  89  PRO B  90  ILE B 149  HOH B2028                    
SITE     1 AC4 11 GLY B  18  THR B  19  ILE C  17  ALA C  38                    
SITE     2 AC4 11 LYS C  40  GLU C  87  TYR C  88  CYS C  89                    
SITE     3 AC4 11 PRO C  90  GLU C  93  ILE C 149                               
CRYST1   66.526   75.410   79.736  86.03  69.05  90.03 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      0.015032  0.000008 -0.005772        0.00000                         
SCALE2      0.000000  0.013261 -0.000988        0.00000                         
SCALE3      0.000000  0.000000  0.013466        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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