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Database: PDB
Entry: 4DAW
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Original site: 4DAW 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       13-JAN-12   4DAW              
TITLE     CRYSTAL STRUCTURE OF PAK1 KINASE DOMAIN WITH THE RUTHENIUM PHTHALIMIDE
TITLE    2 COMPLEX                                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SERINE/THREONINE-PROTEIN KINASE PAK 1;                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 249-545;                                      
COMPND   5 SYNONYM: ALPHA-PAK, P21-ACTIVATED KINASE 1, PAK-1, P65-PAK;          
COMPND   6 EC: 2.7.11.1;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: PAK1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    SERINE/THREONINE KINASE, PHOSPHORYLATION, ATP-BINDING, TRANSFERASE-   
KEYWDS   2 TRANSFERASE INHIBITOR COMPLEX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.MAKSIMOSKA,R.MARMORSTEIN                                            
REVDAT   2   30-MAY-12 4DAW    1       JRNL                                     
REVDAT   1   14-MAR-12 4DAW    0                                                
JRNL        AUTH   S.BLANCK,J.MAKSIMOSKA,J.BAUMEISTER,K.HARMS,R.MARMORSTEIN,    
JRNL        AUTH 2 E.MEGGERS                                                    
JRNL        TITL   THE ART OF FILLING PROTEIN POCKETS EFFICIENTLY WITH          
JRNL        TITL 2 OCTAHEDRAL METAL COMPLEXES.                                  
JRNL        REF    ANGEW.CHEM.INT.ED.ENGL.       V.  51  5244 2012              
JRNL        REFN                   ISSN 1433-7851                               
JRNL        PMID   22383326                                                     
JRNL        DOI    10.1002/ANIE.201108865                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 27.95                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 21570                          
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1163                            
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) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1535                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.33                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2210                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 90                           
REMARK   3   BIN FREE R VALUE                    : 0.2740                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2259                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 30                                      
REMARK   3   SOLVENT ATOMS            : 205                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.50                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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): 0.193         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.166         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.108         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.735         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.914                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2390 ; 0.009 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3263 ; 1.373 ; 2.003       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   311 ; 5.401 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    93 ;39.585 ;25.161       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   426 ;15.373 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;22.875 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   378 ; 0.076 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1752 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1126 ; 0.192 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1659 ; 0.298 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   181 ; 0.120 ; 0.200       
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):    29 ; 0.162 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    22 ; 0.161 ; 0.200       
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):  1538 ; 0.602 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2420 ; 1.026 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1040 ; 1.389 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   831 ; 2.282 ; 4.500       
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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 4DAW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JAN-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB070100.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-FEB-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X6A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.98                               
REMARK 200  MONOCHROMATOR                  : SI (111)                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 270                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 22771                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.13700                            
REMARK 200  R SYM                      (I) : 0.09800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.58700                            
REMARK 200  R SYM FOR SHELL            (I) : 0.56100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3FXZ                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.03                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.46                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25 PEG 4000, 1 M NACL, 10 MM DTT, 0.1    
REMARK 280  M HEPES, PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       61.39500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       61.39500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       25.83800            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       51.77450            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       25.83800            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       51.77450            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       61.39500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       25.83800            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       51.77450            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       61.39500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       25.83800            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       51.77450            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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 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     ASN A   543                                                      
REMARK 465     ASN A   544                                                      
REMARK 465     HIS A   545                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASP A 250    CG   OD1  OD2                                       
REMARK 470     GLU A 251    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 268    CG   CD   CE   NZ                                   
REMARK 470     GLU A 274    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 275    CD   CE   NZ                                        
REMARK 470     GLN A 278    CG   CD   OE1  NE2                                  
REMARK 470     GLN A 304    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 338    CG   OD1  OD2                                       
REMARK 470     GLN A 418    CG   CD   OE1  NE2                                  
REMARK 470     ARG A 438    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A 466    CG   OD1  ND2                                       
REMARK 470     GLU A 483    CD   OE1  OE2                                       
REMARK 470     LYS A 489    CE   NZ                                             
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    ARG A 388       -0.37     75.51                                   
REMARK 500    ASP A 407       87.65     68.39                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0H2 A 601                 
DBREF  4DAW A  249   545  UNP    Q13153   PAK1_HUMAN     249    545             
SEQADV 4DAW ARG A  299  UNP  Q13153    LYS   299 ENGINEERED MUTATION            
SEQRES   1 A  297  SER ASP GLU GLU ILE LEU GLU LYS LEU ARG SER ILE VAL          
SEQRES   2 A  297  SER VAL GLY ASP PRO LYS LYS LYS TYR THR ARG PHE GLU          
SEQRES   3 A  297  LYS ILE GLY GLN GLY ALA SER GLY THR VAL TYR THR ALA          
SEQRES   4 A  297  MET ASP VAL ALA THR GLY GLN GLU VAL ALA ILE ARG GLN          
SEQRES   5 A  297  MET ASN LEU GLN GLN GLN PRO LYS LYS GLU LEU ILE ILE          
SEQRES   6 A  297  ASN GLU ILE LEU VAL MET ARG GLU ASN LYS ASN PRO ASN          
SEQRES   7 A  297  ILE VAL ASN TYR LEU ASP SER TYR LEU VAL GLY ASP GLU          
SEQRES   8 A  297  LEU TRP VAL VAL MET GLU TYR LEU ALA GLY GLY SER LEU          
SEQRES   9 A  297  THR ASP VAL VAL THR GLU THR CYS MET ASP GLU GLY GLN          
SEQRES  10 A  297  ILE ALA ALA VAL CYS ARG GLU CYS LEU GLN ALA LEU GLU          
SEQRES  11 A  297  PHE LEU HIS SER ASN GLN VAL ILE HIS ARG ASP ILE LYS          
SEQRES  12 A  297  SER ASP ASN ILE LEU LEU GLY MET ASP GLY SER VAL LYS          
SEQRES  13 A  297  LEU THR ASP PHE GLY PHE CYS ALA GLN ILE THR PRO GLU          
SEQRES  14 A  297  GLN SER LYS ARG SER TPO MET VAL GLY THR PRO TYR TRP          
SEQRES  15 A  297  MET ALA PRO GLU VAL VAL THR ARG LYS ALA TYR GLY PRO          
SEQRES  16 A  297  LYS VAL ASP ILE TRP SER LEU GLY ILE MET ALA ILE GLU          
SEQRES  17 A  297  MET ILE GLU GLY GLU PRO PRO TYR LEU ASN GLU ASN PRO          
SEQRES  18 A  297  LEU ARG ALA LEU TYR LEU ILE ALA THR ASN GLY THR PRO          
SEQRES  19 A  297  GLU LEU GLN ASN PRO GLU LYS LEU SER ALA ILE PHE ARG          
SEQRES  20 A  297  ASP PHE LEU ASN ARG CYS LEU GLU MET ASP VAL GLU LYS          
SEQRES  21 A  297  ARG GLY SER ALA LYS GLU LEU LEU GLN HIS GLN PHE LEU          
SEQRES  22 A  297  LYS ILE ALA LYS PRO LEU SER SER LEU THR PRO LEU ILE          
SEQRES  23 A  297  ALA ALA ALA LYS GLU ALA THR LYS ASN ASN HIS                  
MODRES 4DAW TPO A  423  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 423      11                                                       
HET    0H2  A 601      30                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     0H2 [1,3-DIOXO-6-(PYRIDIN-2-YL-KAPPAN)-2,3-DIHYDRO-1H-               
HETNAM   2 0H2  ISOINDOL-5-YL-KAPPAC~5~][(THIOXOMETHYLIDENE)AZANIDO-            
HETNAM   3 0H2  KAPPAN](1,4,7-TRITHIONANE-KAPPA~3~S~1~,S~4~,S~7~)               
HETNAM   4 0H2  RUTHENIUM                                                       
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   2  0H2    C20 H19 N3 O2 RU S4                                          
FORMUL   3  HOH   *205(H2 O)                                                    
HELIX    1   1 SER A  249  VAL A  261  1                                  13    
HELIX    2   2 ASP A  265  LYS A  268  5                                   4    
HELIX    3   3 GLN A  304  GLN A  306  5                                   3    
HELIX    4   4 LYS A  308  ASN A  322  1                                  15    
HELIX    5   5 SER A  351  THR A  359  1                                   9    
HELIX    6   6 ASP A  362  ASN A  383  1                                  22    
HELIX    7   7 LYS A  391  ASP A  393  5                                   3    
HELIX    8   8 THR A  427  ALA A  432  5                                   6    
HELIX    9   9 PRO A  433  ARG A  438  1                                   6    
HELIX   10  10 PRO A  443  GLY A  460  1                                  18    
HELIX   11  11 ASN A  468  GLY A  480  1                                  13    
HELIX   12  12 ASN A  486  LEU A  490  5                                   5    
HELIX   13  13 SER A  491  LEU A  502  1                                  12    
HELIX   14  14 SER A  511  LEU A  516  1                                   6    
HELIX   15  15 GLN A  517  ALA A  524  5                                   8    
HELIX   16  16 PRO A  526  SER A  529  5                                   4    
HELIX   17  17 LEU A  530  THR A  541  1                                  12    
SHEET    1   A 5 TYR A 270  GLY A 279  0                                        
SHEET    2   A 5 GLY A 282  ASP A 289 -1  O  MET A 288   N  THR A 271           
SHEET    3   A 5 GLU A 295  ASN A 302 -1  O  GLN A 300   N  THR A 283           
SHEET    4   A 5 GLU A 339  GLU A 345 -1  O  MET A 344   N  ALA A 297           
SHEET    5   A 5 TYR A 330  VAL A 336 -1  N  ASP A 332   O  VAL A 343           
SHEET    1   B 2 VAL A 385  ILE A 386  0                                        
SHEET    2   B 2 ALA A 412  GLN A 413 -1  O  ALA A 412   N  ILE A 386           
SHEET    1   C 2 ILE A 395  LEU A 397  0                                        
SHEET    2   C 2 VAL A 403  LEU A 405 -1  O  LYS A 404   N  LEU A 396           
LINK         C   SER A 422                 N   TPO A 423     1555   1555  1.33  
LINK         C   TPO A 423                 N   MET A 424     1555   1555  1.33  
SITE     1 AC1 15 ILE A 276  SER A 281  GLY A 282  VAL A 284                    
SITE     2 AC1 15 ALA A 297  ARG A 299  VAL A 328  MET A 344                    
SITE     3 AC1 15 GLU A 345  TYR A 346  LEU A 347  LEU A 396                    
SITE     4 AC1 15 THR A 406  ASP A 407  HOH A 758                               
CRYST1   51.676  103.549  122.790  90.00  90.00  90.00 C 2 2 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      0.019351  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009657  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008144        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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