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Database: PDB
Entry: 4L0N
LinkDB: 4L0N
Original site: 4L0N 
HEADER    TRANSFERASE                             31-MAY-13   4L0N              
TITLE     CRYSTAL STRUCTURE OF STK3 (MST2) SARAH DOMAIN                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE 3;                         
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J;                                 
COMPND   4 FRAGMENT: SARAH DOMAIN (UNP RESIDUES 436-484);                       
COMPND   5 SYNONYM: MAMMALIAN STE20-LIKE PROTEIN KINASE 2, MST-2, STE20-LIKE    
COMPND   6 KINASE MST2, SERINE/THREONINE-PROTEIN KINASE KRS-1, SERINE/THREONINE-
COMPND   7 PROTEIN KINASE 3 36KDA SUBUNIT, MST2/N, SERINE/THREONINE-PROTEIN     
COMPND   8 KINASE 3 20KDA SUBUNIT, MST2/C;                                      
COMPND   9 EC: 2.7.11.1;                                                        
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: KRS1, MST2, STK3;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)-R3;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PNIC28-BSA4                               
KEYWDS    STRUCTURAL GENOMICS, STRUCTURAL GENOMICS CONSORTIUM, SGC, SARAH       
KEYWDS   2 DOMAIN, STK3, MST2, HEPTAD REPEAT, STRUCTURAL GENOMICS CONSORTIUM    
KEYWDS   3 (SGC), TRANSFERASE                                                   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.CHAIKUAD,T.KROJER,J.A.NEWMAN,S.DIXON-CLARKE,F.VON DELFT,            
AUTHOR   2 C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,S.KNAPP,STRUCTURAL GENOMICS     
AUTHOR   3 CONSORTIUM (SGC)                                                     
REVDAT   2   28-FEB-24 4L0N    1       SEQADV                                   
REVDAT   1   19-JUN-13 4L0N    0                                                
JRNL        AUTH   A.CHAIKUAD,T.KROJER,J.A.NEWMAN,S.DIXON-CLARKE,F.VON DELFT,   
JRNL        AUTH 2 C.H.ARROWSMITH,A.M.EDWARDS,C.BOUNTRA,S.KNAPP,                
JRNL        AUTH 3 STRUCTURAL GENOMICS CONSORTIUM (SGC)                         
JRNL        TITL   CRYSTAL STRUCTURE OF STK3 (MST2) SARAH DOMAIN                
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
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) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.66                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 108637                         
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) : 0.163                           
REMARK   3   R VALUE            (WORKING SET) : 0.160                           
REMARK   3   FREE R VALUE                     : 0.207                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5733                            
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) : 1.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.44                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 7849                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.57                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2040                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 422                          
REMARK   3   BIN FREE R VALUE                    : 0.2640                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4225                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 799                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.17                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.46000                                              
REMARK   3    B22 (A**2) : 0.46000                                              
REMARK   3    B33 (A**2) : -0.91000                                             
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): 0.067         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.065         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.041         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.284         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.958                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4572 ; 0.017 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  4632 ; 0.001 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6142 ; 1.718 ; 2.025       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 10724 ; 0.805 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   573 ; 4.773 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   245 ;29.375 ;24.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1036 ;13.654 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    58 ;14.563 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   667 ; 0.095 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5065 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   981 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2118 ; 2.638 ; 1.785       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2117 ; 2.638 ; 1.785       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2648 ; 3.098 ; 2.673       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2454 ; 3.877 ; 2.231       
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):  9204 ; 4.883 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   237 ;30.990 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  9687 ;10.761 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : 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 4L0N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JUN-13.                  
REMARK 100 THE DEPOSITION ID IS D_1000080031.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-APR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 4.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I02                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : SI (111) DOUBLE CRYSTAL            
REMARK 200                                   MONOCHROMATOR                      
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 114371                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 32.840                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 5.400                              
REMARK 200  R MERGE                    (I) : 0.06700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.48                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.54400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHARP                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% MPD, 0.1M ACETATE PH 4.9, 0.2M       
REMARK 280  CALCIUM CHLORIDE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE        
REMARK 280  277.15K                                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
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   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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      150.93000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       30.66000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       30.66000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       75.46500            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       30.66000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       30.66000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      226.39500            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       30.66000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       30.66000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       75.46500            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       30.66000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       30.66000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      226.39500            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      150.93000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6                                        
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: 2820 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7450 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2900 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7390 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
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: 2760 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7600 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2830 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7670 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H                                  
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: 5                                                       
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: 2580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7940 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I                                     
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   BIOMT1   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      150.93000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
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: 2450 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 7390 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: J                                     
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   BIOMT1   2  0.000000 -1.000000  0.000000       61.32000            
REMARK 350   BIOMT2   2 -1.000000  0.000000  0.000000       61.32000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      150.93000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH C 548  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH C 565  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     SER J   434                                                      
REMARK 465     MET J   435                                                      
REMARK 465     ASP J   436                                                      
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 F 484    CG   CD   CE   NZ                                   
REMARK 470     MET G   0    CG   SD   CE                                        
REMARK 470     ASP G 438    CG   OD1  OD2                                       
REMARK 470     LYS G 441    CD   CE   NZ                                        
REMARK 470     ASN G 442    CG   OD1  ND2                                       
REMARK 470     ASP H 436    CG   OD1  OD2                                       
REMARK 470     PHE J 437    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP J 438    CG   OD1  OD2                                       
REMARK 470     LYS J 441    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    HOH F   562     O    HOH F   568              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 474   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    MET B 481   CG  -  SD  -  CE  ANGL. DEV. = -10.8 DEGREES          
REMARK 500    MET D 458   CG  -  SD  -  CE  ANGL. DEV. =  11.0 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    MET G   0      -16.57   -142.78                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4L0N A  436   484  UNP    Q13188   STK3_HUMAN     436    484             
DBREF  4L0N B  436   484  UNP    Q13188   STK3_HUMAN     436    484             
DBREF  4L0N C  436   484  UNP    Q13188   STK3_HUMAN     436    484             
DBREF  4L0N D  436   484  UNP    Q13188   STK3_HUMAN     436    484             
DBREF  4L0N E  436   484  UNP    Q13188   STK3_HUMAN     436    484             
DBREF  4L0N F  436   484  UNP    Q13188   STK3_HUMAN     436    484             
DBREF  4L0N G  436   484  UNP    Q13188   STK3_HUMAN     436    484             
DBREF  4L0N H  436   484  UNP    Q13188   STK3_HUMAN     436    484             
DBREF  4L0N I  436   484  UNP    Q13188   STK3_HUMAN     436    484             
DBREF  4L0N J  436   484  UNP    Q13188   STK3_HUMAN     436    484             
SEQADV 4L0N SER A   -1  UNP  Q13188              EXPRESSION TAG                 
SEQADV 4L0N MET A    0  UNP  Q13188              EXPRESSION TAG                 
SEQADV 4L0N SER B   -1  UNP  Q13188              EXPRESSION TAG                 
SEQADV 4L0N MET B    0  UNP  Q13188              EXPRESSION TAG                 
SEQADV 4L0N SER C   -1  UNP  Q13188              EXPRESSION TAG                 
SEQADV 4L0N MET C    0  UNP  Q13188              EXPRESSION TAG                 
SEQADV 4L0N SER D   -1  UNP  Q13188              EXPRESSION TAG                 
SEQADV 4L0N MET D    0  UNP  Q13188              EXPRESSION TAG                 
SEQADV 4L0N SER E   -1  UNP  Q13188              EXPRESSION TAG                 
SEQADV 4L0N MET E    0  UNP  Q13188              EXPRESSION TAG                 
SEQADV 4L0N SER F   -1  UNP  Q13188              EXPRESSION TAG                 
SEQADV 4L0N MET F    0  UNP  Q13188              EXPRESSION TAG                 
SEQADV 4L0N SER G   -1  UNP  Q13188              EXPRESSION TAG                 
SEQADV 4L0N MET G    0  UNP  Q13188              EXPRESSION TAG                 
SEQADV 4L0N SER H   -1  UNP  Q13188              EXPRESSION TAG                 
SEQADV 4L0N MET H    0  UNP  Q13188              EXPRESSION TAG                 
SEQADV 4L0N SER I   -1  UNP  Q13188              EXPRESSION TAG                 
SEQADV 4L0N MET I    0  UNP  Q13188              EXPRESSION TAG                 
SEQADV 4L0N SER J  434  UNP  Q13188              EXPRESSION TAG                 
SEQADV 4L0N MET J  435  UNP  Q13188              EXPRESSION TAG                 
SEQRES   1 A   51  SER MET ASP PHE ASP PHE LEU LYS ASN LEU SER LEU GLU          
SEQRES   2 A   51  GLU LEU GLN MET ARG LEU LYS ALA LEU ASP PRO MET MET          
SEQRES   3 A   51  GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR THR ALA          
SEQRES   4 A   51  LYS ARG GLN PRO ILE LEU ASP ALA MET ASP ALA LYS              
SEQRES   1 B   51  SER MET ASP PHE ASP PHE LEU LYS ASN LEU SER LEU GLU          
SEQRES   2 B   51  GLU LEU GLN MET ARG LEU LYS ALA LEU ASP PRO MET MET          
SEQRES   3 B   51  GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR THR ALA          
SEQRES   4 B   51  LYS ARG GLN PRO ILE LEU ASP ALA MET ASP ALA LYS              
SEQRES   1 C   51  SER MET ASP PHE ASP PHE LEU LYS ASN LEU SER LEU GLU          
SEQRES   2 C   51  GLU LEU GLN MET ARG LEU LYS ALA LEU ASP PRO MET MET          
SEQRES   3 C   51  GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR THR ALA          
SEQRES   4 C   51  LYS ARG GLN PRO ILE LEU ASP ALA MET ASP ALA LYS              
SEQRES   1 D   51  SER MET ASP PHE ASP PHE LEU LYS ASN LEU SER LEU GLU          
SEQRES   2 D   51  GLU LEU GLN MET ARG LEU LYS ALA LEU ASP PRO MET MET          
SEQRES   3 D   51  GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR THR ALA          
SEQRES   4 D   51  LYS ARG GLN PRO ILE LEU ASP ALA MET ASP ALA LYS              
SEQRES   1 E   51  SER MET ASP PHE ASP PHE LEU LYS ASN LEU SER LEU GLU          
SEQRES   2 E   51  GLU LEU GLN MET ARG LEU LYS ALA LEU ASP PRO MET MET          
SEQRES   3 E   51  GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR THR ALA          
SEQRES   4 E   51  LYS ARG GLN PRO ILE LEU ASP ALA MET ASP ALA LYS              
SEQRES   1 F   51  SER MET ASP PHE ASP PHE LEU LYS ASN LEU SER LEU GLU          
SEQRES   2 F   51  GLU LEU GLN MET ARG LEU LYS ALA LEU ASP PRO MET MET          
SEQRES   3 F   51  GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR THR ALA          
SEQRES   4 F   51  LYS ARG GLN PRO ILE LEU ASP ALA MET ASP ALA LYS              
SEQRES   1 G   51  SER MET ASP PHE ASP PHE LEU LYS ASN LEU SER LEU GLU          
SEQRES   2 G   51  GLU LEU GLN MET ARG LEU LYS ALA LEU ASP PRO MET MET          
SEQRES   3 G   51  GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR THR ALA          
SEQRES   4 G   51  LYS ARG GLN PRO ILE LEU ASP ALA MET ASP ALA LYS              
SEQRES   1 H   51  SER MET ASP PHE ASP PHE LEU LYS ASN LEU SER LEU GLU          
SEQRES   2 H   51  GLU LEU GLN MET ARG LEU LYS ALA LEU ASP PRO MET MET          
SEQRES   3 H   51  GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR THR ALA          
SEQRES   4 H   51  LYS ARG GLN PRO ILE LEU ASP ALA MET ASP ALA LYS              
SEQRES   1 I   51  SER MET ASP PHE ASP PHE LEU LYS ASN LEU SER LEU GLU          
SEQRES   2 I   51  GLU LEU GLN MET ARG LEU LYS ALA LEU ASP PRO MET MET          
SEQRES   3 I   51  GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR THR ALA          
SEQRES   4 I   51  LYS ARG GLN PRO ILE LEU ASP ALA MET ASP ALA LYS              
SEQRES   1 J   51  SER MET ASP PHE ASP PHE LEU LYS ASN LEU SER LEU GLU          
SEQRES   2 J   51  GLU LEU GLN MET ARG LEU LYS ALA LEU ASP PRO MET MET          
SEQRES   3 J   51  GLU ARG GLU ILE GLU GLU LEU ARG GLN ARG TYR THR ALA          
SEQRES   4 J   51  LYS ARG GLN PRO ILE LEU ASP ALA MET ASP ALA LYS              
FORMUL  11  HOH   *799(H2 O)                                                    
HELIX    1   1 SER A   -1  LYS A  441  1                                   8    
HELIX    2   2 SER A  444  LYS A  484  1                                  41    
HELIX    3   3 MET B    0  LEU B  443  1                                   9    
HELIX    4   4 SER B  444  ALA B  483  1                                  40    
HELIX    5   5 ASP C  436  LYS C  441  1                                   6    
HELIX    6   6 SER C  444  ALA C  483  1                                  40    
HELIX    7   7 MET D    0  LYS D  441  1                                   7    
HELIX    8   8 SER D  444  ALA D  483  1                                  40    
HELIX    9   9 ASP E  436  LYS E  441  1                                   6    
HELIX   10  10 SER E  444  ALA E  483  1                                  40    
HELIX   11  11 MET F    0  LYS F  441  1                                   7    
HELIX   12  12 SER F  444  ALA F  483  1                                  40    
HELIX   13  13 MET G    0  LEU G  440  1                                   6    
HELIX   14  14 LYS G  441  LEU G  443  5                                   3    
HELIX   15  15 SER G  444  ALA G  483  1                                  40    
HELIX   16  16 MET H    0  LYS H  441  1                                   7    
HELIX   17  17 SER H  444  ALA H  483  1                                  40    
HELIX   18  18 MET I    0  LYS I  441  1                                   7    
HELIX   19  19 SER I  444  ALA I  483  1                                  40    
HELIX   20  20 SER J  444  LYS J  484  1                                  41    
CRYST1   61.320   61.320  301.860  90.00  90.00  90.00 P 41 21 2    80          
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      0.016308  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.016308  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003313        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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