GenomeNet

Database: PDB
Entry: 4B9D
LinkDB: 4B9D
Original site: 4B9D 
HEADER    TRANSFERASE                             04-SEP-12   4B9D              
TITLE     CRYSTAL STRUCTURE OF HUMAN NIMA-RELATED KINASE 1 (NEK1) WITH          
TITLE    2 INHIBITOR.                                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE NEK1;                      
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: KINASE DOMAIN, RESIDUES 1-328;                             
COMPND   5 SYNONYM: NIMA-RELATED KINASE 1, NEVER IN MITOSIS A-RELATED KINASE 1, 
COMPND   6 NIMA-RELATED PROTEIN KINASE 1, RENAL CARCINOMA ANTIGEN NY-REN-55;    
COMPND   7 EC: 2.7.11.1;                                                        
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 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 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    TRANSFERASE, INHIBITOR                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.M.ELKINS,T.D.M.HANCHUK,D.V.LOVATO,F.L.BASEI,G.V.MEIRELLES,J.KOBARG, 
AUTHOR   2 M.SZKLARZ,M.VOLLMAR,P.MAHAJAN,P.RELLOS,Y.ZHANG,T.KROJER,A.C.W.PIKE,  
AUTHOR   3 P.CANNING,F.VON DELFT,J.RAYNOR,C.BOUNTRA,C.ARROWSMITH,A.EDWARDS,     
AUTHOR   4 S.KNAPP                                                              
REVDAT   3   12-AUG-20 4B9D    1       JRNL   REMARK                            
REVDAT   2   24-JAN-18 4B9D    1       AUTHOR JRNL                              
REVDAT   1   19-SEP-12 4B9D    0                                                
JRNL        AUTH   T.D.MELO-HANCHUK,P.F.SLEPICKA,G.V.MEIRELLES,F.L.BASEI,       
JRNL        AUTH 2 D.V.LOVATO,D.C.GRANATO,B.A.PAULETTI,R.R.DOMINGUES,           
JRNL        AUTH 3 A.F.P.LEME,A.L.PELEGRINI,G.LENZ,S.KNAPP,J.M.ELKINS,J.KOBARG  
JRNL        TITL   NEK1 KINASE DOMAIN STRUCTURE AND ITS DYNAMIC PROTEIN         
JRNL        TITL 2 INTERACTOME AFTER EXPOSURE TO CISPLATIN.                     
JRNL        REF    SCI REP                       V.   7  5445 2017              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   28710492                                                     
JRNL        DOI    10.1038/S41598-017-05325-W                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.22                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 49632                          
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) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2593                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3557                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.47                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3070                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 186                          
REMARK   3   BIN FREE R VALUE                    : 0.3210                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4648                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 53                                      
REMARK   3   SOLVENT ATOMS            : 234                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.60                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.25000                                             
REMARK   3    B22 (A**2) : 0.47000                                              
REMARK   3    B33 (A**2) : 0.78000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.157         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.138         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.094         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 6.281         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.940                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4843 ; 0.013 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4634 ; 0.004 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6542 ; 1.500 ; 1.971       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10611 ; 0.983 ; 3.003       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   593 ; 5.861 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   224 ;36.413 ;23.571       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   864 ;13.702 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    35 ;21.106 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   722 ; 0.084 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5461 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1162 ; 0.004 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 1                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     A   -20    283       B   -20    283   17394  0.08  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    -7        A    83                          
REMARK   3    ORIGIN FOR THE GROUP (A):  14.1840  -1.2800 -27.1410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1612 T22:   0.1053                                     
REMARK   3      T33:   0.0978 T12:   0.0342                                     
REMARK   3      T13:  -0.0088 T23:   0.0170                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2162 L22:   6.7194                                     
REMARK   3      L33:   2.0176 L12:   0.1967                                     
REMARK   3      L13:   0.1250 L23:   3.0686                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0650 S12:   0.1183 S13:   0.0161                       
REMARK   3      S21:  -0.6231 S22:   0.0462 S23:  -0.0778                       
REMARK   3      S31:  -0.1549 S32:   0.0917 S33:   0.0188                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    84        A   328                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.6410  22.6720 -20.2080              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1343 T22:   0.0407                                     
REMARK   3      T33:   0.0659 T12:   0.0481                                     
REMARK   3      T13:   0.0189 T23:  -0.0050                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4598 L22:   1.6362                                     
REMARK   3      L33:   2.3957 L12:  -0.1781                                     
REMARK   3      L13:  -0.4950 L23:   0.1121                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2259 S12:   0.0343 S13:   0.2581                       
REMARK   3      S21:  -0.0904 S22:  -0.1664 S23:   0.0914                       
REMARK   3      S31:  -0.4455 S32:  -0.1129 S33:  -0.0595                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    -7        B    83                          
REMARK   3    ORIGIN FOR THE GROUP (A):  46.6280  15.5030 -67.6770              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0825 T22:   0.1382                                     
REMARK   3      T33:   0.0772 T12:   0.0082                                     
REMARK   3      T13:   0.0011 T23:   0.0009                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.8624 L22:   0.4841                                     
REMARK   3      L33:   2.5068 L12:   0.4579                                     
REMARK   3      L13:  -2.2496 L23:  -0.0553                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1300 S12:   0.6660 S13:   0.0477                       
REMARK   3      S21:  -0.0350 S22:  -0.0214 S23:   0.0334                       
REMARK   3      S31:  -0.2118 S32:  -0.1211 S33:  -0.1086                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    84        B   328                          
REMARK   3    ORIGIN FOR THE GROUP (A):  22.7950  21.3920 -61.8060              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0410 T22:   0.1160                                     
REMARK   3      T33:   0.0425 T12:  -0.0038                                     
REMARK   3      T13:   0.0131 T23:   0.0109                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9752 L22:   1.8347                                     
REMARK   3      L33:   1.6284 L12:   0.3439                                     
REMARK   3      L13:   0.3514 L23:  -0.0083                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0880 S12:   0.0971 S13:   0.0156                       
REMARK   3      S21:   0.0139 S22:   0.0645 S23:   0.2216                       
REMARK   3      S31:  -0.0673 S32:  -0.1558 S33:   0.0234                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS.                                                          
REMARK   4                                                                      
REMARK   4 4B9D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-SEP-12.                  
REMARK 100 THE DEPOSITION ID IS D_1290053876.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-MAR-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9173                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC CCD                           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52249                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.180                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY                : 4.300                              
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.94                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: PDB ENTRY 4APC                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M NA/KPO4, 20% PEG 3350, 10%          
REMARK 280  ETHYLENE GLYCOL, PH 7.5                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       82.48000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       82.48000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       45.18000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       46.83000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       45.18000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       46.83000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       82.48000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       45.18000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       46.83000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       82.48000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       45.18000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       46.83000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1570 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29520 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.8 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A   -21                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     SER A   -14                                                      
REMARK 465     SER A   -13                                                      
REMARK 465     GLY A   -12                                                      
REMARK 465     VAL A   -11                                                      
REMARK 465     ASP A   -10                                                      
REMARK 465     LEU A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     GLY A    11                                                      
REMARK 465     GLU A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     PHE A    15                                                      
REMARK 465     GLY A    16                                                      
REMARK 465     SER A   285                                                      
REMARK 465     GLN A   286                                                      
REMARK 465     PRO A   287                                                      
REMARK 465     ILE A   288                                                      
REMARK 465     PRO A   289                                                      
REMARK 465     ALA A   290                                                      
REMARK 465     LYS A   291                                                      
REMARK 465     ARG A   292                                                      
REMARK 465     PRO A   293                                                      
REMARK 465     ALA A   294                                                      
REMARK 465     SER A   295                                                      
REMARK 465     GLY A   296                                                      
REMARK 465     GLN A   297                                                      
REMARK 465     ASN A   298                                                      
REMARK 465     SER A   299                                                      
REMARK 465     ILE A   300                                                      
REMARK 465     SER A   301                                                      
REMARK 465     VAL A   302                                                      
REMARK 465     MET A   303                                                      
REMARK 465     PRO A   304                                                      
REMARK 465     ALA A   305                                                      
REMARK 465     GLN A   306                                                      
REMARK 465     LYS A   307                                                      
REMARK 465     ILE A   308                                                      
REMARK 465     THR A   309                                                      
REMARK 465     LYS A   310                                                      
REMARK 465     PRO A   311                                                      
REMARK 465     ALA A   312                                                      
REMARK 465     ALA A   313                                                      
REMARK 465     LYS A   314                                                      
REMARK 465     TYR A   315                                                      
REMARK 465     GLY A   316                                                      
REMARK 465     ILE A   317                                                      
REMARK 465     PRO A   318                                                      
REMARK 465     LEU A   319                                                      
REMARK 465     ALA A   320                                                      
REMARK 465     TYR A   321                                                      
REMARK 465     LYS A   322                                                      
REMARK 465     LYS A   323                                                      
REMARK 465     TYR A   324                                                      
REMARK 465     GLY A   325                                                      
REMARK 465     ASP A   326                                                      
REMARK 465     LYS A   327                                                      
REMARK 465     LYS A   328                                                      
REMARK 465     MET B   -21                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     SER B   -14                                                      
REMARK 465     SER B   -13                                                      
REMARK 465     GLY B   -12                                                      
REMARK 465     GLU B    12                                                      
REMARK 465     GLY B    13                                                      
REMARK 465     SER B    14                                                      
REMARK 465     PHE B    15                                                      
REMARK 465     GLY B    16                                                      
REMARK 465     SER B   285                                                      
REMARK 465     GLN B   286                                                      
REMARK 465     PRO B   287                                                      
REMARK 465     ILE B   288                                                      
REMARK 465     PRO B   289                                                      
REMARK 465     ALA B   290                                                      
REMARK 465     LYS B   291                                                      
REMARK 465     ARG B   292                                                      
REMARK 465     PRO B   293                                                      
REMARK 465     ALA B   294                                                      
REMARK 465     SER B   295                                                      
REMARK 465     GLY B   296                                                      
REMARK 465     GLN B   297                                                      
REMARK 465     ASN B   298                                                      
REMARK 465     SER B   299                                                      
REMARK 465     ILE B   300                                                      
REMARK 465     SER B   301                                                      
REMARK 465     VAL B   302                                                      
REMARK 465     MET B   303                                                      
REMARK 465     PRO B   304                                                      
REMARK 465     ALA B   305                                                      
REMARK 465     GLN B   306                                                      
REMARK 465     LYS B   307                                                      
REMARK 465     ILE B   308                                                      
REMARK 465     THR B   309                                                      
REMARK 465     LYS B   310                                                      
REMARK 465     PRO B   311                                                      
REMARK 465     ALA B   312                                                      
REMARK 465     ALA B   313                                                      
REMARK 465     LYS B   314                                                      
REMARK 465     TYR B   315                                                      
REMARK 465     GLY B   316                                                      
REMARK 465     ILE B   317                                                      
REMARK 465     PRO B   318                                                      
REMARK 465     LEU B   319                                                      
REMARK 465     ALA B   320                                                      
REMARK 465     TYR B   321                                                      
REMARK 465     LYS B   322                                                      
REMARK 465     LYS B   323                                                      
REMARK 465     TYR B   324                                                      
REMARK 465     GLY B   325                                                      
REMARK 465     ASP B   326                                                      
REMARK 465     LYS B   327                                                      
REMARK 465     LYS B   328                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     HIS A -20    CG   ND1  CD2  CE1  NE2                             
REMARK 470     HIS A -19    CG   ND1  CD2  CE1  NE2                             
REMARK 470     HIS A -18    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A   9    CD   CE   NZ                                        
REMARK 470     LYS A  17    CG   CD   CE   NZ                                   
REMARK 470     LYS A  22    CG   CD   CE   NZ                                   
REMARK 470     LYS A  33    CD   CE   NZ                                        
REMARK 470     SER A  42    OG                                                  
REMARK 470     LYS A  43    CD   CE   NZ                                        
REMARK 470     GLU A  44    CD   OE1  OE2                                       
REMARK 470     GLU A  46    CG   CD   OE1  OE2                                  
REMARK 470     ARG A  50    NE   CZ   NH1  NH2                                  
REMARK 470     LYS A  59    NZ                                                  
REMARK 470     LYS A  90    CE   NZ                                             
REMARK 470     LYS A  96    CE   NZ                                             
REMARK 470     LYS A 200    NZ                                                  
REMARK 470     ARG A 241    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLY A 284    C    O                                              
REMARK 470     HIS B -20    CG   ND1  CD2  CE1  NE2                             
REMARK 470     VAL B -11    CG1  CG2                                            
REMARK 470     ASP B -10    CG   OD1  OD2                                       
REMARK 470     LYS B   9    CD   CE   NZ                                        
REMARK 470     LYS B  17    CD   CE   NZ                                        
REMARK 470     SER B  42    OG                                                  
REMARK 470     LYS B  43    CG   CD   CE   NZ                                   
REMARK 470     GLU B  46    CD   OE1  OE2                                       
REMARK 470     LYS B  59    CE   NZ                                             
REMARK 470     GLN B  65    CD   OE1  NE2                                       
REMARK 470     LYS B  90    CD   CE   NZ                                        
REMARK 470     LYS B  96    CE   NZ                                             
REMARK 470     LYS B 138    CD   CE   NZ                                        
REMARK 470     LYS B 178    CE   NZ                                             
REMARK 470     LYS B 200    CE   NZ                                             
REMARK 470     GLU B 204    CD   OE1  OE2                                       
REMARK 470     GLN B 237    CD   OE1  NE2                                       
REMARK 470     ARG B 241    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASN B   242     O    HOH B  2117              1.95            
REMARK 500   O    HOH A  2012     O    HOH A  2080              2.07            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS A 163   CA  -  CB  -  SG  ANGL. DEV. =  14.4 DEGREES          
REMARK 500    CYS A 276   CA  -  CB  -  SG  ANGL. DEV. =   6.7 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLN A   8      142.95   -174.02                                   
REMARK 500    GLU A  25      -71.18    -59.60                                   
REMARK 500    SER A  41     -179.78    -68.15                                   
REMARK 500    HIS B -19       98.22    -65.56                                   
REMARK 500    GLN B   8      143.25   -173.90                                   
REMARK 500    SER B  41     -179.97    -68.08                                   
REMARK 500    CYS B 276      -53.35   -127.68                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CK7 A 1285                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1286                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL A 1287                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CK7 B 1285                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 1286                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 1287                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4APC   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN NIMA-RELATED KINASE 1 (NEK1)              
DBREF  4B9D A    1   328  UNP    Q96PY6   NEK1_HUMAN       1    328             
DBREF  4B9D B    1   328  UNP    Q96PY6   NEK1_HUMAN       1    328             
SEQADV 4B9D MET A  -21  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D HIS A  -20  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D HIS A  -19  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D HIS A  -18  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D HIS A  -17  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D HIS A  -16  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D HIS A  -15  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D SER A  -14  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D SER A  -13  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D GLY A  -12  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D VAL A  -11  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D ASP A  -10  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D LEU A   -9  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D GLY A   -8  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D THR A   -7  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D GLU A   -6  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D ASN A   -5  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D LEU A   -4  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D TYR A   -3  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D PHE A   -2  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D GLN A   -1  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D SER A    0  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D ALA A  162  UNP  Q96PY6    THR   162 ENGINEERED MUTATION            
SEQADV 4B9D MET B  -21  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D HIS B  -20  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D HIS B  -19  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D HIS B  -18  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D HIS B  -17  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D HIS B  -16  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D HIS B  -15  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D SER B  -14  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D SER B  -13  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D GLY B  -12  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D VAL B  -11  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D ASP B  -10  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D LEU B   -9  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D GLY B   -8  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D THR B   -7  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D GLU B   -6  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D ASN B   -5  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D LEU B   -4  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D TYR B   -3  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D PHE B   -2  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D GLN B   -1  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D SER B    0  UNP  Q96PY6              EXPRESSION TAG                 
SEQADV 4B9D ALA B  162  UNP  Q96PY6    THR   162 ENGINEERED MUTATION            
SEQRES   1 A  350  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  350  GLY THR GLU ASN LEU TYR PHE GLN SER MET GLU LYS TYR          
SEQRES   3 A  350  VAL ARG LEU GLN LYS ILE GLY GLU GLY SER PHE GLY LYS          
SEQRES   4 A  350  ALA ILE LEU VAL LYS SER THR GLU ASP GLY ARG GLN TYR          
SEQRES   5 A  350  VAL ILE LYS GLU ILE ASN ILE SER ARG MET SER SER LYS          
SEQRES   6 A  350  GLU ARG GLU GLU SER ARG ARG GLU VAL ALA VAL LEU ALA          
SEQRES   7 A  350  ASN MET LYS HIS PRO ASN ILE VAL GLN TYR ARG GLU SER          
SEQRES   8 A  350  PHE GLU GLU ASN GLY SER LEU TYR ILE VAL MET ASP TYR          
SEQRES   9 A  350  CYS GLU GLY GLY ASP LEU PHE LYS ARG ILE ASN ALA GLN          
SEQRES  10 A  350  LYS GLY VAL LEU PHE GLN GLU ASP GLN ILE LEU ASP TRP          
SEQRES  11 A  350  PHE VAL GLN ILE CYS LEU ALA LEU LYS HIS VAL HIS ASP          
SEQRES  12 A  350  ARG LYS ILE LEU HIS ARG ASP ILE LYS SER GLN ASN ILE          
SEQRES  13 A  350  PHE LEU THR LYS ASP GLY THR VAL GLN LEU GLY ASP PHE          
SEQRES  14 A  350  GLY ILE ALA ARG VAL LEU ASN SER THR VAL GLU LEU ALA          
SEQRES  15 A  350  ARG ALA CYS ILE GLY THR PRO TYR TYR LEU SER PRO GLU          
SEQRES  16 A  350  ILE CYS GLU ASN LYS PRO TYR ASN ASN LYS SER ASP ILE          
SEQRES  17 A  350  TRP ALA LEU GLY CYS VAL LEU TYR GLU LEU CYS THR LEU          
SEQRES  18 A  350  LYS HIS ALA PHE GLU ALA GLY SER MET LYS ASN LEU VAL          
SEQRES  19 A  350  LEU LYS ILE ILE SER GLY SER PHE PRO PRO VAL SER LEU          
SEQRES  20 A  350  HIS TYR SER TYR ASP LEU ARG SER LEU VAL SER GLN LEU          
SEQRES  21 A  350  PHE LYS ARG ASN PRO ARG ASP ARG PRO SER VAL ASN SER          
SEQRES  22 A  350  ILE LEU GLU LYS GLY PHE ILE ALA LYS ARG ILE GLU LYS          
SEQRES  23 A  350  PHE LEU SER PRO GLN LEU ILE ALA GLU GLU PHE CYS LEU          
SEQRES  24 A  350  LYS THR PHE SER LYS PHE GLY SER GLN PRO ILE PRO ALA          
SEQRES  25 A  350  LYS ARG PRO ALA SER GLY GLN ASN SER ILE SER VAL MET          
SEQRES  26 A  350  PRO ALA GLN LYS ILE THR LYS PRO ALA ALA LYS TYR GLY          
SEQRES  27 A  350  ILE PRO LEU ALA TYR LYS LYS TYR GLY ASP LYS LYS              
SEQRES   1 B  350  MET HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  350  GLY THR GLU ASN LEU TYR PHE GLN SER MET GLU LYS TYR          
SEQRES   3 B  350  VAL ARG LEU GLN LYS ILE GLY GLU GLY SER PHE GLY LYS          
SEQRES   4 B  350  ALA ILE LEU VAL LYS SER THR GLU ASP GLY ARG GLN TYR          
SEQRES   5 B  350  VAL ILE LYS GLU ILE ASN ILE SER ARG MET SER SER LYS          
SEQRES   6 B  350  GLU ARG GLU GLU SER ARG ARG GLU VAL ALA VAL LEU ALA          
SEQRES   7 B  350  ASN MET LYS HIS PRO ASN ILE VAL GLN TYR ARG GLU SER          
SEQRES   8 B  350  PHE GLU GLU ASN GLY SER LEU TYR ILE VAL MET ASP TYR          
SEQRES   9 B  350  CYS GLU GLY GLY ASP LEU PHE LYS ARG ILE ASN ALA GLN          
SEQRES  10 B  350  LYS GLY VAL LEU PHE GLN GLU ASP GLN ILE LEU ASP TRP          
SEQRES  11 B  350  PHE VAL GLN ILE CYS LEU ALA LEU LYS HIS VAL HIS ASP          
SEQRES  12 B  350  ARG LYS ILE LEU HIS ARG ASP ILE LYS SER GLN ASN ILE          
SEQRES  13 B  350  PHE LEU THR LYS ASP GLY THR VAL GLN LEU GLY ASP PHE          
SEQRES  14 B  350  GLY ILE ALA ARG VAL LEU ASN SER THR VAL GLU LEU ALA          
SEQRES  15 B  350  ARG ALA CYS ILE GLY THR PRO TYR TYR LEU SER PRO GLU          
SEQRES  16 B  350  ILE CYS GLU ASN LYS PRO TYR ASN ASN LYS SER ASP ILE          
SEQRES  17 B  350  TRP ALA LEU GLY CYS VAL LEU TYR GLU LEU CYS THR LEU          
SEQRES  18 B  350  LYS HIS ALA PHE GLU ALA GLY SER MET LYS ASN LEU VAL          
SEQRES  19 B  350  LEU LYS ILE ILE SER GLY SER PHE PRO PRO VAL SER LEU          
SEQRES  20 B  350  HIS TYR SER TYR ASP LEU ARG SER LEU VAL SER GLN LEU          
SEQRES  21 B  350  PHE LYS ARG ASN PRO ARG ASP ARG PRO SER VAL ASN SER          
SEQRES  22 B  350  ILE LEU GLU LYS GLY PHE ILE ALA LYS ARG ILE GLU LYS          
SEQRES  23 B  350  PHE LEU SER PRO GLN LEU ILE ALA GLU GLU PHE CYS LEU          
SEQRES  24 B  350  LYS THR PHE SER LYS PHE GLY SER GLN PRO ILE PRO ALA          
SEQRES  25 B  350  LYS ARG PRO ALA SER GLY GLN ASN SER ILE SER VAL MET          
SEQRES  26 B  350  PRO ALA GLN LYS ILE THR LYS PRO ALA ALA LYS TYR GLY          
SEQRES  27 B  350  ILE PRO LEU ALA TYR LYS LYS TYR GLY ASP LYS LYS              
HET    CK7  A1285      23                                                       
HET     CL  A1286       1                                                       
HET     CL  A1287       1                                                       
HET    CK7  B1285      23                                                       
HET     CL  B1286       1                                                       
HET    EDO  B1287       4                                                       
HETNAM     CK7 [4-(2-AMINO-4-METHYL-THIAZOL-5-YL)-PYRIMIDIN-2-YL]-(3-           
HETNAM   2 CK7  NITRO-PHENYL)-AMINE                                             
HETNAM      CL CHLORIDE ION                                                     
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   3  CK7    2(C14 H12 N6 O2 S)                                           
FORMUL   4   CL    3(CL 1-)                                                     
FORMUL   8  EDO    C2 H6 O2                                                     
FORMUL   9  HOH   *234(H2 O)                                                    
HELIX    1   1 SER A   41  MET A   58  1                                  18    
HELIX    2   2 ASP A   87  GLN A   95  1                                   9    
HELIX    3   3 GLN A  101  ARG A  122  1                                  22    
HELIX    4   4 LYS A  130  GLN A  132  5                                   3    
HELIX    5   5 ASN A  154  GLY A  165  1                                  12    
HELIX    6   6 SER A  171  GLU A  176  1                                   6    
HELIX    7   7 ASN A  181  LEU A  199  1                                  19    
HELIX    8   8 SER A  207  GLY A  218  1                                  12    
HELIX    9   9 SER A  228  PHE A  239  1                                  12    
HELIX   10  10 ASN A  242  ARG A  246  5                                   5    
HELIX   11  11 SER A  248  GLU A  254  1                                   7    
HELIX   12  12 LYS A  255  LYS A  260  1                                   6    
HELIX   13  13 ARG A  261  PHE A  265  5                                   5    
HELIX   14  14 SER A  267  CYS A  276  1                                  10    
HELIX   15  15 SER B   41  MET B   58  1                                  18    
HELIX   16  16 ASP B   87  GLN B   95  1                                   9    
HELIX   17  17 GLN B  101  ARG B  122  1                                  22    
HELIX   18  18 LYS B  130  GLN B  132  5                                   3    
HELIX   19  19 ASN B  154  GLY B  165  1                                  12    
HELIX   20  20 SER B  171  GLU B  176  1                                   6    
HELIX   21  21 ASN B  181  LEU B  199  1                                  19    
HELIX   22  22 SER B  207  GLY B  218  1                                  12    
HELIX   23  23 SER B  228  PHE B  239  1                                  12    
HELIX   24  24 ASN B  242  ARG B  246  5                                   5    
HELIX   25  25 SER B  248  LYS B  255  1                                   8    
HELIX   26  26 LYS B  255  LYS B  260  1                                   6    
HELIX   27  27 ARG B  261  PHE B  265  5                                   5    
HELIX   28  28 SER B  267  CYS B  276  1                                  10    
SHEET    1  AA 5 TYR A   4  LYS A   9  0                                        
SHEET    2  AA 5 ALA A  18  SER A  23 -1  O  LEU A  20   N  LEU A   7           
SHEET    3  AA 5 GLN A  29  ASN A  36 -1  O  TYR A  30   N  VAL A  21           
SHEET    4  AA 5 SER A  75  ASP A  81 -1  O  LEU A  76   N  ILE A  35           
SHEET    5  AA 5 TYR A  66  GLU A  72 -1  N  ARG A  67   O  VAL A  79           
SHEET    1  AB 2 LEU A 125  HIS A 126  0                                        
SHEET    2  AB 2 ILE A 149  ALA A 150 -1  O  ALA A 150   N  LEU A 125           
SHEET    1  AC 2 ILE A 134  LEU A 136  0                                        
SHEET    2  AC 2 VAL A 142  LEU A 144 -1  O  GLN A 143   N  PHE A 135           
SHEET    1  BA 5 TYR B   4  LYS B   9  0                                        
SHEET    2  BA 5 ALA B  18  SER B  23 -1  O  LEU B  20   N  LEU B   7           
SHEET    3  BA 5 GLN B  29  ASN B  36 -1  O  TYR B  30   N  VAL B  21           
SHEET    4  BA 5 SER B  75  ASP B  81 -1  O  LEU B  76   N  ILE B  35           
SHEET    5  BA 5 TYR B  66  GLU B  72 -1  N  ARG B  67   O  VAL B  79           
SHEET    1  BB 2 LEU B 125  HIS B 126  0                                        
SHEET    2  BB 2 ILE B 149  ALA B 150 -1  O  ALA B 150   N  LEU B 125           
SHEET    1  BC 2 ILE B 134  LEU B 136  0                                        
SHEET    2  BC 2 VAL B 142  LEU B 144 -1  O  GLN B 143   N  PHE B 135           
SSBOND   1 CYS A  163    CYS B  276                          1555   1555  2.09  
SSBOND   2 CYS A  276    CYS B  163                          1555   6555  2.04  
SITE     1 AC1 11 ALA A  18  MET A  80  ASP A  81  TYR A  82                    
SITE     2 AC1 11 CYS A  83  GLY A  86  ASP A  87  PHE A 135                    
SITE     3 AC1 11 HOH A2039  HOH A2049  HOH A2107                               
SITE     1 AC2  1 ARG A 244                                                     
SITE     1 AC3  4 HIS A 120  ASN A 182  SER A 248  VAL A 249                    
SITE     1 AC4 10 ALA B  18  LYS B  33  MET B  80  ASP B  81                    
SITE     2 AC4 10 TYR B  82  CYS B  83  GLY B  86  ASP B  87                    
SITE     3 AC4 10 PHE B 135  HOH B2051                                          
SITE     1 AC5  4 HIS B 120  ASN B 182  SER B 248  VAL B 249                    
SITE     1 AC6  3 LYS B  59  HIS B  60  PRO B  61                               
CRYST1   90.360   93.660  164.960  90.00  90.00  90.00 C 2 2 21     16          
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      0.011067  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010677  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006062        0.00000                         
MTRIX1   1  0.061840  0.998030  0.010310       -3.35015    1                    
MTRIX2   1 -0.997050  0.062240 -0.044860       41.35561    1                    
MTRIX3   1 -0.045410 -0.007500  0.998940       42.56198    1                    
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system