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Database: PDB
Entry: 3FXZ
LinkDB: 3FXZ
Original site: 3FXZ 
HEADER    TRANSFERASE                             21-JAN-09   3FXZ              
TITLE     CRYSTAL STRUCTURE OF PAK1 KINASE DOMAIN WITH RUTHENIUM                
TITLE    2 COMPLEX LAMBDA-FL172                                                 
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: P21-ACTIVATED KINASE 1, PAK-1, P65-PAK, ALPHA-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: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET151/D-TOPO                             
KEYWDS    TRANSFERASE, KINASE, ATP-BINDING, PHOSPHORYLATION,                    
KEYWDS   2 ALLOSTERIC ENZYME, ALTERNATIVE SPLICING, APOPTOSIS, CELL             
KEYWDS   3 JUNCTION, CYTOPLASM, NUCLEOTIDE-BINDING, PHOSPHOPROTEIN,             
KEYWDS   4 POLYMORPHISM, SERINE/THREONINE-PROTEIN KINASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.MAKSIMOSKA,R.MARMORSTEIN,E.MEGGERS                                  
REVDAT   1   17-FEB-09 3FXZ    0                                                
JRNL        AUTH   J.MAKSIMOSKA,L.FENG,K.HARMS,C.YI,J.KISSIL,                   
JRNL        AUTH 2 R.MARMORSTEIN,E.MEGGERS                                      
JRNL        TITL   TARGETING LARGE KINASE ACTIVE SITE WITH RIGID,               
JRNL        TITL 2 BULKY OCTAHEDRAL RUTHENIUM COMPLEXES                         
JRNL        REF    J.AM.CHEM.SOC.                V. 130 15764 2008              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   18973295                                                     
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.64 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) : 1.64                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 26.38                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 38092                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.196                           
REMARK   3   R VALUE            (WORKING SET) : 0.195                           
REMARK   3   FREE R VALUE                     : 0.218                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2019                            
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) : 1.64                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2441                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 87.27                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2670                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 143                          
REMARK   3   BIN FREE R VALUE                    : 0.2860                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2267                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 42                                      
REMARK   3   SOLVENT ATOMS            : 230                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 30.06                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.15000                                             
REMARK   3    B22 (A**2) : 0.14000                                              
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): 0.099         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.095         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.060         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.324         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.946                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2361 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3231 ; 1.324 ; 2.015       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   304 ; 5.412 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    90 ;37.899 ;24.889       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   413 ;12.520 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;24.542 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   371 ; 0.090 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1745 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1118 ; 0.202 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1644 ; 0.306 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   192 ; 0.152 ; 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):    38 ; 0.218 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    18 ; 0.190 ; 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):  1522 ; 2.061 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2389 ; 2.782 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1119 ; 2.441 ; 2.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   833 ; 3.515 ; 3.000       
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):     1 ;11.793 ; 3.000       
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   : 1.40                                          
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          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3FXZ COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-JAN-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB051178.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-APR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : 8.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-B                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40150                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.640                              
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     (%) : 98.7                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : 0.07700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.64                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.71                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.53300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.000                              
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: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.42                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.48                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS PH 8.0, 1M NACL, 25% PEG       
REMARK 280  4000, 10MM DTT, 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       61.32650            
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       61.32650            
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       26.09150            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       51.73750            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       26.09150            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       51.73750            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       61.32650            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       26.09150            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       51.73750            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       61.32650            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       26.09150            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       51.73750            
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 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 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     LYS A   542                                                      
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 267    CD   CE   NZ                                        
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     MET A 288    CG   SD   CE                                        
REMARK 470     GLN A 304    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 310    CG   CD   OE1  OE2                                  
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     GLU A 507    CG   CD   OE1  OE2                                  
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 A    65     O    HOH A   190              2.14            
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    THR A 271      -80.96   -115.55                                   
REMARK 500    ARG A 388       -1.51     75.86                                   
REMARK 500    ASP A 389       49.11   -141.79                                   
REMARK 500    ASP A 407       85.99     67.32                                   
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 FLL A 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3FY0   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PAK1 KINASE DOMAIN WITH RUTHENIUM               
REMARK 900 COMPLEX DW2                                                          
DBREF  3FXZ A  249   545  UNP    Q13153   PAK1_HUMAN     249    545             
SEQADV 3FXZ ARG A  299  UNP  Q13153    LYS   299 ENGINEERED                     
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 3FXZ TPO A  423  THR  PHOSPHOTHREONINE                                   
HET    TPO  A 423      11                                                       
HET    FLL  A   1      42                                                       
HETNAM     TPO PHOSPHOTHREONINE                                                 
HETNAM     FLL OCTAHEDRAL RU-PYRIDOCARBAZOLE                                    
HETSYN     TPO PHOSPHONOTHREONINE                                               
FORMUL   1  TPO    C4 H10 N O6 P                                                
FORMUL   2  FLL    C30 H18 CL F N5 O4 RU                                        
FORMUL   3  HOH   *230(H2 O)                                                    
HELIX    1   1 SER A  249  VAL A  261  1                                  13    
HELIX    2   2 ASP A  265  LYS A  269  5                                   5    
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  MET A  431  5                                   5    
HELIX    9   9 ALA A  432  ARG A  438  1                                   7    
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 GLU A 274  GLY A 279  0                                        
SHEET    2   A 5 GLY A 282  MET A 288 -1  O  VAL A 284   N  ILE A 276           
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 17 HOH A  50  HOH A  68  ILE A 276  GLY A 277                    
SITE     2 AC1 17 GLN A 278  VAL A 284  ALA A 297  ARG A 299                    
SITE     3 AC1 17 MET A 344  GLU A 345  TYR A 346  LEU A 347                    
SITE     4 AC1 17 ALA A 348  GLY A 350  ASP A 393  ASN A 394                    
SITE     5 AC1 17 LEU A 396                                                     
CRYST1   52.183  103.475  122.653  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      0.019163  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009664  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008153        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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