GenomeNet

Database: PDB
Entry: 3COM
LinkDB: 3COM
Original site: 3COM 
HEADER    TRANSFERASE                             28-MAR-08   3COM              
TITLE     CRYSTAL STRUCTURE OF MST1 KINASE                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE 4;                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: PROTEIN KINASE DOMAIN: RESIDUES 2-311;                     
COMPND   5 SYNONYM: STE20-LIKE KINASE MST1, MST-1, MAMMALIAN STE20-LIKE PROTEIN 
COMPND   6 KINASE 1, SERINE/THREONINE-PROTEIN KINASE KRS-2;                     
COMPND   7 EC: 2.7.11.1;                                                        
COMPND   8 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: STK4, MST1;                                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PSGX4                                     
KEYWDS    KINASE, MST1, SERINE/THREONINE-PROTEIN KINASE 4, STE20-LIKE KINASE,   
KEYWDS   2 PSI, STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE, NEW YORK SGX 
KEYWDS   3 RESEARCH CENTER FOR STRUCTURAL GENOMICS, NYSGXRC, ALTERNATIVE        
KEYWDS   4 SPLICING, APOPTOSIS, ATP-BINDING, COILED COIL, CYTOPLASM, MAGNESIUM, 
KEYWDS   5 METAL-BINDING, NUCLEOTIDE-BINDING, NUCLEUS, PHOSPHOPROTEIN,          
KEYWDS   6 POLYMORPHISM, TRANSFERASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.ATWELL,S.K.BURLEY,M.DICKEY,B.LEON,J.M.SAUDER,NEW YORK SGX RESEARCH  
AUTHOR   2 CENTER FOR STRUCTURAL GENOMICS (NYSGXRC)                             
REVDAT   6   14-NOV-18 3COM    1       AUTHOR                                   
REVDAT   5   25-OCT-17 3COM    1       REMARK                                   
REVDAT   4   09-JUN-09 3COM    1       REVDAT                                   
REVDAT   3   24-FEB-09 3COM    1       VERSN                                    
REVDAT   2   23-DEC-08 3COM    1       AUTHOR KEYWDS                            
REVDAT   1   15-APR-08 3COM    0                                                
JRNL        AUTH   S.ATWELL,S.K.BURLEY,M.DICKEY,B.LEON,J.M.SAUDER               
JRNL        TITL   CRYSTAL STRUCTURE OF MST1 KINASE.                            
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.0                                           
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 40443                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.208                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.244                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2022                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE SET COUNT          : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4283                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 231                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : NULL                          
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : NULL                          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  NULL ; 0.015 ;  NULL       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  NULL ; 1.394 ;  NULL       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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   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 : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : NULL                                          
REMARK   3   ION PROBE RADIUS   : NULL                                          
REMARK   3   SHRINKAGE RADIUS   : NULL                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3COM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-APR-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000047028.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-JUN-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 10.5                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 31-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9794                             
REMARK 200  MONOCHROMATOR                  : KOHZU 111 DIAMOND                  
REMARK 200  OPTICS                         : KV MIRRORS                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40513                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 90.2                               
REMARK 200  DATA REDUNDANCY                : 3.200                              
REMARK 200  R MERGE                    (I) : 0.11800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3CKW                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 59.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1700MM AMMONIUM SULFATE, 300MM LITHIUM   
REMARK 280  SULFATE, 100MM CAPS PH 10.5, VAPOR DIFFUSION, SITTING DROP,         
REMARK 280  TEMPERATURE 294K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   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       37.48850            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       55.47750            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.57550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       55.47750            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       37.48850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.57550            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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     SER A     0                                                      
REMARK 465     LEU A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     ARG A     7                                                      
REMARK 465     ASN A     8                                                      
REMARK 465     PRO A     9                                                      
REMARK 465     PRO A    10                                                      
REMARK 465     ARG A    11                                                      
REMARK 465     ARG A    12                                                      
REMARK 465     GLN A    13                                                      
REMARK 465     LEU A    14                                                      
REMARK 465     LYS A    15                                                      
REMARK 465     LYS A    16                                                      
REMARK 465     LEU A    17                                                      
REMARK 465     ASP A    18                                                      
REMARK 465     GLU A    19                                                      
REMARK 465     ASP A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     LEU A    22                                                      
REMARK 465     THR A    23                                                      
REMARK 465     LYS A    24                                                      
REMARK 465     GLN A    25                                                      
REMARK 465     PRO A    26                                                      
REMARK 465     GLU A    27                                                      
REMARK 465     GLU A    28                                                      
REMARK 465     GLU A    38                                                      
REMARK 465     GLY A    39                                                      
REMARK 465     SER A    40                                                      
REMARK 465     TYR A    41                                                      
REMARK 465     ASP A   299                                                      
REMARK 465     VAL A   300                                                      
REMARK 465     LYS A   301                                                      
REMARK 465     LEU A   302                                                      
REMARK 465     LYS A   303                                                      
REMARK 465     ARG A   304                                                      
REMARK 465     GLN A   305                                                      
REMARK 465     GLU A   306                                                      
REMARK 465     SER A   307                                                      
REMARK 465     GLN A   308                                                      
REMARK 465     GLN A   309                                                      
REMARK 465     ARG A   310                                                      
REMARK 465     GLU A   311                                                      
REMARK 465     GLU A   312                                                      
REMARK 465     GLY A   313                                                      
REMARK 465     SER B     0                                                      
REMARK 465     LEU B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     GLN B     5                                                      
REMARK 465     LEU B     6                                                      
REMARK 465     ARG B     7                                                      
REMARK 465     ASN B     8                                                      
REMARK 465     PRO B     9                                                      
REMARK 465     PRO B    10                                                      
REMARK 465     ARG B    11                                                      
REMARK 465     ARG B    12                                                      
REMARK 465     GLN B    13                                                      
REMARK 465     LEU B    14                                                      
REMARK 465     LYS B    15                                                      
REMARK 465     GLU B    38                                                      
REMARK 465     GLY B    39                                                      
REMARK 465     SER B    40                                                      
REMARK 465     TYR B    41                                                      
REMARK 465     LYS B   301                                                      
REMARK 465     LEU B   302                                                      
REMARK 465     LYS B   303                                                      
REMARK 465     ARG B   304                                                      
REMARK 465     GLN B   305                                                      
REMARK 465     GLU B   306                                                      
REMARK 465     SER B   307                                                      
REMARK 465     GLN B   308                                                      
REMARK 465     GLN B   309                                                      
REMARK 465     ARG B   310                                                      
REMARK 465     GLU B   311                                                      
REMARK 465     GLU B   312                                                      
REMARK 465     GLY B   313                                                      
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     GLU A  34    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  35    CG   CD   CE   NZ                                   
REMARK 470     GLU A  51    CG   CD   OE1  OE2                                  
REMARK 470     GLN A  60    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  94    CG   CD   CE   NZ                                   
REMARK 470     GLU A 160    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 198    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 246    CE   NZ                                             
REMARK 470     GLU B  27    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  34    CG   CD   OE1  OE2                                  
REMARK 470     LYS B  35    CG   CD   CE   NZ                                   
REMARK 470     LYS B  59    CG   CD   CE   NZ                                   
REMARK 470     ASN B  95    CG   OD1  ND2                                       
REMARK 470     ASN B 182    CG   OD1  ND2                                       
REMARK 470     GLU B 198    CG   CD   OE1  OE2                                  
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    ASP A 167   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP A 206   CB  -  CG  -  OD2 ANGL. DEV. =   6.1 DEGREES          
REMARK 500    ASP A 256   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP B  81   CB  -  CG  -  OD2 ANGL. DEV. =   5.7 DEGREES          
REMARK 500    ASP B 124   CB  -  CG  -  OD2 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ARG B 144   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG B 144   NE  -  CZ  -  NH2 ANGL. DEV. =   3.3 DEGREES          
REMARK 500    ASP B 206   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP B 256   CB  -  CG  -  OD2 ANGL. DEV. =   5.9 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    LEU A  33     -113.96   -103.00                                   
REMARK 500    GLU A  64       46.87    -78.36                                   
REMARK 500    ARG A 148       -9.10     78.48                                   
REMARK 500    ASP A 167       69.76     66.24                                   
REMARK 500    ASN A 202     -157.33   -132.46                                   
REMARK 500    LEU A 262       50.16   -104.35                                   
REMARK 500    SER B  65     -157.31   -157.73                                   
REMARK 500    ASN B  95       70.29     41.37                                   
REMARK 500    THR B  96       -1.98     70.40                                   
REMARK 500    ARG B 148       -1.11     70.25                                   
REMARK 500    ASP B 167       78.39     67.00                                   
REMARK 500    ASN B 202     -157.82   -133.69                                   
REMARK 500    LEU B 262       51.37    -96.04                                   
REMARK 500    ASP B 299      -71.95    -53.36                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: NYSGXRC-8191A   RELATED DB: TARGETDB                     
DBREF  3COM A    2   311  UNP    Q13043   STK4_HUMAN       2    311             
DBREF  3COM B    2   311  UNP    Q13043   STK4_HUMAN       2    311             
SEQADV 3COM SER A    0  UNP  Q13043              EXPRESSION TAG                 
SEQADV 3COM LEU A    1  UNP  Q13043              EXPRESSION TAG                 
SEQADV 3COM GLU A  312  UNP  Q13043              EXPRESSION TAG                 
SEQADV 3COM GLY A  313  UNP  Q13043              EXPRESSION TAG                 
SEQADV 3COM SER B    0  UNP  Q13043              EXPRESSION TAG                 
SEQADV 3COM LEU B    1  UNP  Q13043              EXPRESSION TAG                 
SEQADV 3COM GLU B  312  UNP  Q13043              EXPRESSION TAG                 
SEQADV 3COM GLY B  313  UNP  Q13043              EXPRESSION TAG                 
SEQRES   1 A  314  SER LEU GLU THR VAL GLN LEU ARG ASN PRO PRO ARG ARG          
SEQRES   2 A  314  GLN LEU LYS LYS LEU ASP GLU ASP SER LEU THR LYS GLN          
SEQRES   3 A  314  PRO GLU GLU VAL PHE ASP VAL LEU GLU LYS LEU GLY GLU          
SEQRES   4 A  314  GLY SER TYR GLY SER VAL TYR LYS ALA ILE HIS LYS GLU          
SEQRES   5 A  314  THR GLY GLN ILE VAL ALA ILE LYS GLN VAL PRO VAL GLU          
SEQRES   6 A  314  SER ASP LEU GLN GLU ILE ILE LYS GLU ILE SER ILE MET          
SEQRES   7 A  314  GLN GLN CYS ASP SER PRO HIS VAL VAL LYS TYR TYR GLY          
SEQRES   8 A  314  SER TYR PHE LYS ASN THR ASP LEU TRP ILE VAL MET GLU          
SEQRES   9 A  314  TYR CYS GLY ALA GLY SER VAL SER ASP ILE ILE ARG LEU          
SEQRES  10 A  314  ARG ASN LYS THR LEU THR GLU ASP GLU ILE ALA THR ILE          
SEQRES  11 A  314  LEU GLN SER THR LEU LYS GLY LEU GLU TYR LEU HIS PHE          
SEQRES  12 A  314  MET ARG LYS ILE HIS ARG ASP ILE LYS ALA GLY ASN ILE          
SEQRES  13 A  314  LEU LEU ASN THR GLU GLY HIS ALA LYS LEU ALA ASP PHE          
SEQRES  14 A  314  GLY VAL ALA GLY GLN LEU THR ASP TPO MET ALA LYS ARG          
SEQRES  15 A  314  ASN TPO VAL ILE GLY THR PRO PHE TRP MET ALA PRO GLU          
SEQRES  16 A  314  VAL ILE GLN GLU ILE GLY TYR ASN CYS VAL ALA ASP ILE          
SEQRES  17 A  314  TRP SER LEU GLY ILE THR ALA ILE GLU MET ALA GLU GLY          
SEQRES  18 A  314  LYS PRO PRO TYR ALA ASP ILE HIS PRO MET ARG ALA ILE          
SEQRES  19 A  314  PHE MET ILE PRO THR ASN PRO PRO PRO THR PHE ARG LYS          
SEQRES  20 A  314  PRO GLU LEU TRP SER ASP ASN PHE THR ASP PHE VAL LYS          
SEQRES  21 A  314  GLN CYS LEU VAL LYS SER PRO GLU GLN ARG ALA THR ALA          
SEQRES  22 A  314  THR GLN LEU LEU GLN HIS PRO PHE VAL ARG SER ALA LYS          
SEQRES  23 A  314  GLY VAL SER ILE LEU ARG ASP LEU ILE ASN GLU ALA MET          
SEQRES  24 A  314  ASP VAL LYS LEU LYS ARG GLN GLU SER GLN GLN ARG GLU          
SEQRES  25 A  314  GLU GLY                                                      
SEQRES   1 B  314  SER LEU GLU THR VAL GLN LEU ARG ASN PRO PRO ARG ARG          
SEQRES   2 B  314  GLN LEU LYS LYS LEU ASP GLU ASP SER LEU THR LYS GLN          
SEQRES   3 B  314  PRO GLU GLU VAL PHE ASP VAL LEU GLU LYS LEU GLY GLU          
SEQRES   4 B  314  GLY SER TYR GLY SER VAL TYR LYS ALA ILE HIS LYS GLU          
SEQRES   5 B  314  THR GLY GLN ILE VAL ALA ILE LYS GLN VAL PRO VAL GLU          
SEQRES   6 B  314  SER ASP LEU GLN GLU ILE ILE LYS GLU ILE SER ILE MET          
SEQRES   7 B  314  GLN GLN CYS ASP SER PRO HIS VAL VAL LYS TYR TYR GLY          
SEQRES   8 B  314  SER TYR PHE LYS ASN THR ASP LEU TRP ILE VAL MET GLU          
SEQRES   9 B  314  TYR CYS GLY ALA GLY SER VAL SER ASP ILE ILE ARG LEU          
SEQRES  10 B  314  ARG ASN LYS THR LEU THR GLU ASP GLU ILE ALA THR ILE          
SEQRES  11 B  314  LEU GLN SER THR LEU LYS GLY LEU GLU TYR LEU HIS PHE          
SEQRES  12 B  314  MET ARG LYS ILE HIS ARG ASP ILE LYS ALA GLY ASN ILE          
SEQRES  13 B  314  LEU LEU ASN THR GLU GLY HIS ALA LYS LEU ALA ASP PHE          
SEQRES  14 B  314  GLY VAL ALA GLY GLN LEU THR ASP TPO MET ALA LYS ARG          
SEQRES  15 B  314  ASN TPO VAL ILE GLY THR PRO PHE TRP MET ALA PRO GLU          
SEQRES  16 B  314  VAL ILE GLN GLU ILE GLY TYR ASN CYS VAL ALA ASP ILE          
SEQRES  17 B  314  TRP SER LEU GLY ILE THR ALA ILE GLU MET ALA GLU GLY          
SEQRES  18 B  314  LYS PRO PRO TYR ALA ASP ILE HIS PRO MET ARG ALA ILE          
SEQRES  19 B  314  PHE MET ILE PRO THR ASN PRO PRO PRO THR PHE ARG LYS          
SEQRES  20 B  314  PRO GLU LEU TRP SER ASP ASN PHE THR ASP PHE VAL LYS          
SEQRES  21 B  314  GLN CYS LEU VAL LYS SER PRO GLU GLN ARG ALA THR ALA          
SEQRES  22 B  314  THR GLN LEU LEU GLN HIS PRO PHE VAL ARG SER ALA LYS          
SEQRES  23 B  314  GLY VAL SER ILE LEU ARG ASP LEU ILE ASN GLU ALA MET          
SEQRES  24 B  314  ASP VAL LYS LEU LYS ARG GLN GLU SER GLN GLN ARG GLU          
SEQRES  25 B  314  GLU GLY                                                      
MODRES 3COM TPO A  177  THR  PHOSPHOTHREONINE                                   
MODRES 3COM TPO A  183  THR  PHOSPHOTHREONINE                                   
MODRES 3COM TPO B  177  THR  PHOSPHOTHREONINE                                   
MODRES 3COM TPO B  183  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 177      11                                                       
HET    TPO  A 183      11                                                       
HET    TPO  B 177      11                                                       
HET    TPO  B 183      11                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    4(C4 H10 N O6 P)                                             
FORMUL   3  HOH   *231(H2 O)                                                    
HELIX    1   1 LEU A   67  GLN A   79  1                                  13    
HELIX    2   2 VAL A  110  ASN A  118  1                                   9    
HELIX    3   3 THR A  122  MET A  143  1                                  22    
HELIX    4   4 LYS A  151  GLY A  153  5                                   3    
HELIX    5   5 THR A  187  MET A  191  5                                   5    
HELIX    6   6 ALA A  192  GLN A  197  1                                   6    
HELIX    7   7 VAL A  204  GLY A  220  1                                  17    
HELIX    8   8 HIS A  228  ASN A  239  1                                  12    
HELIX    9   9 LYS A  246  TRP A  250  5                                   5    
HELIX   10  10 SER A  251  LEU A  262  1                                  12    
HELIX   11  11 THR A  271  LEU A  276  1                                   6    
HELIX   12  12 HIS A  278  SER A  283  1                                   6    
HELIX   13  13 GLY A  286  ILE A  289  5                                   4    
HELIX   14  14 LEU A  290  MET A  298  1                                   9    
HELIX   15  15 ASP B   18  THR B   23  1                                   6    
HELIX   16  16 GLN B   25  VAL B   29  1                                   5    
HELIX   17  17 ASP B   66  GLN B   78  1                                  13    
HELIX   18  18 VAL B  110  ASN B  118  1                                   9    
HELIX   19  19 THR B  122  MET B  143  1                                  22    
HELIX   20  20 LYS B  151  GLY B  153  5                                   3    
HELIX   21  21 THR B  187  MET B  191  5                                   5    
HELIX   22  22 ALA B  192  GLN B  197  1                                   6    
HELIX   23  23 VAL B  204  GLY B  220  1                                  17    
HELIX   24  24 HIS B  228  ILE B  236  1                                   9    
HELIX   25  25 LYS B  246  TRP B  250  5                                   5    
HELIX   26  26 SER B  251  LEU B  262  1                                  12    
HELIX   27  27 THR B  271  LEU B  276  1                                   6    
HELIX   28  28 HIS B  278  SER B  283  1                                   6    
HELIX   29  29 GLY B  286  ILE B  289  5                                   4    
HELIX   30  30 LEU B  290  VAL B  300  1                                  11    
SHEET    1   A 5 PHE A  30  LYS A  35  0                                        
SHEET    2   A 5 SER A  43  HIS A  49 -1  O  LYS A  46   N  LEU A  33           
SHEET    3   A 5 ILE A  55  PRO A  62 -1  O  GLN A  60   N  SER A  43           
SHEET    4   A 5 ASP A  97  GLU A 103 -1  O  LEU A  98   N  VAL A  61           
SHEET    5   A 5 TYR A  88  LYS A  94 -1  N  TYR A  89   O  VAL A 101           
SHEET    1   B 3 GLY A 108  SER A 109  0                                        
SHEET    2   B 3 ILE A 155  LEU A 157 -1  O  LEU A 157   N  GLY A 108           
SHEET    3   B 3 ALA A 163  LEU A 165 -1  O  LYS A 164   N  LEU A 156           
SHEET    1   C 2 LYS A 145  ILE A 146  0                                        
SHEET    2   C 2 GLY A 172  GLN A 173 -1  O  GLY A 172   N  ILE A 146           
SHEET    1   D 5 PHE B  30  LYS B  35  0                                        
SHEET    2   D 5 VAL B  44  HIS B  49 -1  O  LYS B  46   N  LEU B  33           
SHEET    3   D 5 ILE B  55  PRO B  62 -1  O  ILE B  58   N  TYR B  45           
SHEET    4   D 5 ASP B  97  GLU B 103 -1  O  LEU B  98   N  VAL B  61           
SHEET    5   D 5 TYR B  88  LYS B  94 -1  N  TYR B  92   O  TRP B  99           
SHEET    1   E 3 GLY B 108  SER B 109  0                                        
SHEET    2   E 3 ILE B 155  LEU B 157 -1  O  LEU B 157   N  GLY B 108           
SHEET    3   E 3 ALA B 163  LEU B 165 -1  O  LYS B 164   N  LEU B 156           
SHEET    1   F 2 LYS B 145  ILE B 146  0                                        
SHEET    2   F 2 GLY B 172  GLN B 173 -1  O  GLY B 172   N  ILE B 146           
LINK         C   ASP A 176                 N   TPO A 177     1555   1555  1.33  
LINK         C   TPO A 177                 N   MET A 178     1555   1555  1.32  
LINK         C   ASN A 182                 N   TPO A 183     1555   1555  1.33  
LINK         C   TPO A 183                 N   VAL A 184     1555   1555  1.33  
LINK         C   ASP B 176                 N   TPO B 177     1555   1555  1.33  
LINK         C   TPO B 177                 N   MET B 178     1555   1555  1.33  
LINK         C   ASN B 182                 N   TPO B 183     1555   1555  1.33  
LINK         C   TPO B 183                 N   VAL B 184     1555   1555  1.34  
CRYST1   74.977  105.151  110.955  90.00  90.00  90.00 P 21 21 21    8          
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      0.013337  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009510  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009013        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system