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Database: PDB
Entry: 3KN5
LinkDB: 3KN5
Original site: 3KN5 
HEADER    TRANSFERASE                             12-NOV-09   3KN5              
TITLE     CRYSTAL STRUCTURE OF THE C-TERMINAL KINASE DOMAIN OF MSK1 IN COMPLEX  
TITLE    2 WITH AMP-PNP                                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RIBOSOMAL PROTEIN S6 KINASE ALPHA-5;                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 FRAGMENT: RESIDUES 414-738;                                          
COMPND   5 SYNONYM: NUCLEAR MITOGEN- AND STRESS-ACTIVATED PROTEIN KINASE 1, 90  
COMPND   6 KDA RIBOSOMAL PROTEIN S6 KINASE 5, RSK-LIKE PROTEIN KINASE, RSKL;    
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: MSK1, RPS6KA5;                                                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21-CODON PLUS (DE3)-RILP;                
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28                                     
KEYWDS    KINASE, AMP-PNP, MSK1, MSK, ATP-BINDING, METAL-BINDING, NUCLEOTIDE-   
KEYWDS   2 BINDING, SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    I.D'ANGELO,M.MALAKHOVA,Z.DONG                                         
REVDAT   3   09-JUN-10 3KN5    1       JRNL                                     
REVDAT   2   12-MAY-10 3KN5    1       JRNL                                     
REVDAT   1   21-APR-10 3KN5    0                                                
JRNL        AUTH   M.MALAKHOVA,I.D'ANGELO,H.G.KIM,I.KURINOV,A.M.BODE,Z.DONG     
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE ACTIVE FORM OF THE C-TERMINAL   
JRNL        TITL 2 KINASE DOMAIN OF MITOGEN- AND STRESS-ACTIVATED PROTEIN       
JRNL        TITL 3 KINASE 1.                                                    
JRNL        REF    J.MOL.BIOL.                   V. 399    41 2010              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   20382163                                                     
JRNL        DOI    10.1016/J.JMB.2010.03.064                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.24                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 23120                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.278                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.130                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1205                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 43.2453 -  4.9819    0.56     2899   148  0.2189 0.2687        
REMARK   3     2  4.9819 -  3.9551    0.54     2757   144  0.1632 0.2312        
REMARK   3     3  3.9551 -  3.4554    0.53     2744   138  0.1827 0.2634        
REMARK   3     4  3.4554 -  3.1396    0.53     2719   147  0.2090 0.2809        
REMARK   3     5  3.1396 -  2.9146    0.52     2619   159  0.2346 0.3623        
REMARK   3     6  2.9146 -  2.7428    0.49     2495   130  0.2475 0.3243        
REMARK   3     7  2.7428 -  2.6055    0.46     2325   140  0.2519 0.2833        
REMARK   3     8  2.6055 -  2.4921    0.41     2116   107  0.2674 0.3434        
REMARK   3     9  2.4921 -  2.3960    0.32     1625    92  0.2756 0.3430        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.35                                          
REMARK   3   B_SOL              : 56.09                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.400            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 63.06                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -13.98100                                            
REMARK   3    B22 (A**2) : 1.31400                                              
REMARK   3    B33 (A**2) : 12.66700                                             
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           4720                                  
REMARK   3   ANGLE     :  1.104           6350                                  
REMARK   3   CHIRALITY :  0.075            691                                  
REMARK   3   PLANARITY :  0.003            793                                  
REMARK   3   DIHEDRAL  : 20.402           1762                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3KN5 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-NOV-08.                  
REMARK 100 THE RCSB ID CODE IS RCSB056199.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 07-MAR-08                          
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               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-C                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0000                             
REMARK 200  MONOCHROMATOR                  : SI(311)                            
REMARK 200  OPTICS                         : MIRROR, MICROFOCUS                 
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23504                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.396                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 43.240                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.11800                            
REMARK 200  R SYM                      (I) : 0.11800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.70                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.49200                            
REMARK 200  R SYM FOR SHELL            (I) : 0.49200                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.800                              
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: 2QR8                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 42.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PH 7.5, VAPOR DIFFUSION                  
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       25.78050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.73000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.62500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       67.73000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.78050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.62500            
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     MET A   414                                                      
REMARK 465     GLU A   555                                                      
REMARK 465     ASN A   556                                                      
REMARK 465     ASP A   557                                                      
REMARK 465     ASN A   558                                                      
REMARK 465     ASP A   575                                                      
REMARK 465     ASN A   576                                                      
REMARK 465     GLN A   577                                                      
REMARK 465     PRO A   578                                                      
REMARK 465     LEU A   579                                                      
REMARK 465     LYS A   580                                                      
REMARK 465     THR A   581                                                      
REMARK 465     PRO A   582                                                      
REMARK 465     CYS A   583                                                      
REMARK 465     PHE A   584                                                      
REMARK 465     THR A   585                                                      
REMARK 465     LEU A   586                                                      
REMARK 465     HIS A   587                                                      
REMARK 465     TYR A   588                                                      
REMARK 465     ALA A   589                                                      
REMARK 465     ALA A   590                                                      
REMARK 465     PRO A   591                                                      
REMARK 465     GLU A   592                                                      
REMARK 465     LEU A   593                                                      
REMARK 465     LEU A   594                                                      
REMARK 465     ASN A   595                                                      
REMARK 465     GLN A   596                                                      
REMARK 465     SER A   624                                                      
REMARK 465     HIS A   625                                                      
REMARK 465     ASP A   626                                                      
REMARK 465     ARG A   627                                                      
REMARK 465     SER A   628                                                      
REMARK 465     LEU A   629                                                      
REMARK 465     THR A   630                                                      
REMARK 465     PHE A   730                                                      
REMARK 465     CYS A   731                                                      
REMARK 465     LEU A   732                                                      
REMARK 465     GLN A   733                                                      
REMARK 465     ASN A   734                                                      
REMARK 465     VAL A   735                                                      
REMARK 465     ASP A   736                                                      
REMARK 465     LYS A   737                                                      
REMARK 465     ALA A   738                                                      
REMARK 465     MET B   414                                                      
REMARK 465     GLU B   555                                                      
REMARK 465     ASN B   556                                                      
REMARK 465     ASP B   557                                                      
REMARK 465     ASN B   558                                                      
REMARK 465     ASP B   575                                                      
REMARK 465     ASN B   576                                                      
REMARK 465     GLN B   577                                                      
REMARK 465     PRO B   578                                                      
REMARK 465     LEU B   579                                                      
REMARK 465     LYS B   580                                                      
REMARK 465     THR B   581                                                      
REMARK 465     PRO B   582                                                      
REMARK 465     CYS B   583                                                      
REMARK 465     PHE B   584                                                      
REMARK 465     THR B   585                                                      
REMARK 465     LEU B   586                                                      
REMARK 465     HIS B   587                                                      
REMARK 465     TYR B   588                                                      
REMARK 465     ALA B   589                                                      
REMARK 465     ALA B   590                                                      
REMARK 465     PRO B   591                                                      
REMARK 465     GLU B   592                                                      
REMARK 465     LEU B   593                                                      
REMARK 465     LEU B   594                                                      
REMARK 465     ASN B   595                                                      
REMARK 465     GLN B   596                                                      
REMARK 465     PHE B   730                                                      
REMARK 465     CYS B   731                                                      
REMARK 465     LEU B   732                                                      
REMARK 465     GLN B   733                                                      
REMARK 465     ASN B   734                                                      
REMARK 465     VAL B   735                                                      
REMARK 465     ASP B   736                                                      
REMARK 465     LYS B   737                                                      
REMARK 465     ALA B   738                                                      
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    VAL B   610     O    HOH B    84              2.08            
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    ASP A 426       78.43   -108.47                                   
REMARK 500    ASN A 449       13.95     59.33                                   
REMARK 500    ASP A 544       40.64   -152.10                                   
REMARK 500    ASP A 565       86.51     65.89                                   
REMARK 500    TYR A 599       95.33    -66.09                                   
REMARK 500    SER A 633      135.38    154.87                                   
REMARK 500    PHE A 648       58.21   -115.18                                   
REMARK 500    ASP A 671      102.91    -34.06                                   
REMARK 500    SER A 707       82.59    146.01                                   
REMARK 500    GLU A 728      -53.34    167.48                                   
REMARK 500    GLU B 434     -157.07   -134.42                                   
REMARK 500    GLU B 476      131.48    -39.45                                   
REMARK 500    ASP B 544       45.91   -151.14                                   
REMARK 500    ASP B 565       80.37     61.12                                   
REMARK 500    ALA B 569      157.46    -49.36                                   
REMARK 500    TYR B 599       90.68    -67.67                                   
REMARK 500    SER B 628     -178.94     92.51                                   
REMARK 500    LEU B 629      -73.36     72.72                                   
REMARK 500    ASP B 645       73.33   -100.62                                   
REMARK 500    ASP B 671     -118.03   -116.47                                   
REMARK 500    ASN B 673       89.95    163.36                                   
REMARK 500    LYS B 674      -86.16     70.79                                   
REMARK 500    SER B 707       34.27   -163.97                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 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,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    LYS B 674        22.8      L          L   OUTSIDE RANGE           
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 ANP A 400                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ANP B 400                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3KN6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE C-TERMINAL KINASE DOMAIN OF MSK1            
DBREF  3KN5 A  414   738  UNP    O75582   KS6A5_HUMAN    414    738             
DBREF  3KN5 B  414   738  UNP    O75582   KS6A5_HUMAN    414    738             
SEQRES   1 A  325  MET LYS ASP SER PRO PHE TYR GLN HIS TYR ASP LEU ASP          
SEQRES   2 A  325  LEU LYS ASP LYS PRO LEU GLY GLU GLY SER PHE SER ILE          
SEQRES   3 A  325  CYS ARG LYS CYS VAL HIS LYS LYS SER ASN GLN ALA PHE          
SEQRES   4 A  325  ALA VAL LYS ILE ILE SER LYS ARG MET GLU ALA ASN THR          
SEQRES   5 A  325  GLN LYS GLU ILE THR ALA LEU LYS LEU CYS GLU GLY HIS          
SEQRES   6 A  325  PRO ASN ILE VAL LYS LEU HIS GLU VAL PHE HIS ASP GLN          
SEQRES   7 A  325  LEU HIS THR PHE LEU VAL MET GLU LEU LEU ASN GLY GLY          
SEQRES   8 A  325  GLU LEU PHE GLU ARG ILE LYS LYS LYS LYS HIS PHE SER          
SEQRES   9 A  325  GLU THR GLU ALA SER TYR ILE MET ARG LYS LEU VAL SER          
SEQRES  10 A  325  ALA VAL SER HIS MET HIS ASP VAL GLY VAL VAL HIS ARG          
SEQRES  11 A  325  ASP LEU LYS PRO GLU ASN LEU LEU PHE THR ASP GLU ASN          
SEQRES  12 A  325  ASP ASN LEU GLU ILE LYS ILE ILE ASP PHE GLY PHE ALA          
SEQRES  13 A  325  ARG LEU LYS PRO PRO ASP ASN GLN PRO LEU LYS THR PRO          
SEQRES  14 A  325  CYS PHE THR LEU HIS TYR ALA ALA PRO GLU LEU LEU ASN          
SEQRES  15 A  325  GLN ASN GLY TYR ASP GLU SER CYS ASP LEU TRP SER LEU          
SEQRES  16 A  325  GLY VAL ILE LEU TYR THR MET LEU SER GLY GLN VAL PRO          
SEQRES  17 A  325  PHE GLN SER HIS ASP ARG SER LEU THR CYS THR SER ALA          
SEQRES  18 A  325  VAL GLU ILE MET LYS LYS ILE LYS LYS GLY ASP PHE SER          
SEQRES  19 A  325  PHE GLU GLY GLU ALA TRP LYS ASN VAL SER GLN GLU ALA          
SEQRES  20 A  325  LYS ASP LEU ILE GLN GLY LEU LEU THR VAL ASP PRO ASN          
SEQRES  21 A  325  LYS ARG LEU LYS MET SER GLY LEU ARG TYR ASN GLU TRP          
SEQRES  22 A  325  LEU GLN ASP GLY SER GLN LEU SER SER ASN PRO LEU MET          
SEQRES  23 A  325  THR PRO ASP ILE LEU GLY SER SER GLY ALA ALA VAL HIS          
SEQRES  24 A  325  THR CYS VAL LYS ALA THR PHE HIS ALA PHE ASN LYS TYR          
SEQRES  25 A  325  LYS ARG GLU GLY PHE CYS LEU GLN ASN VAL ASP LYS ALA          
SEQRES   1 B  325  MET LYS ASP SER PRO PHE TYR GLN HIS TYR ASP LEU ASP          
SEQRES   2 B  325  LEU LYS ASP LYS PRO LEU GLY GLU GLY SER PHE SER ILE          
SEQRES   3 B  325  CYS ARG LYS CYS VAL HIS LYS LYS SER ASN GLN ALA PHE          
SEQRES   4 B  325  ALA VAL LYS ILE ILE SER LYS ARG MET GLU ALA ASN THR          
SEQRES   5 B  325  GLN LYS GLU ILE THR ALA LEU LYS LEU CYS GLU GLY HIS          
SEQRES   6 B  325  PRO ASN ILE VAL LYS LEU HIS GLU VAL PHE HIS ASP GLN          
SEQRES   7 B  325  LEU HIS THR PHE LEU VAL MET GLU LEU LEU ASN GLY GLY          
SEQRES   8 B  325  GLU LEU PHE GLU ARG ILE LYS LYS LYS LYS HIS PHE SER          
SEQRES   9 B  325  GLU THR GLU ALA SER TYR ILE MET ARG LYS LEU VAL SER          
SEQRES  10 B  325  ALA VAL SER HIS MET HIS ASP VAL GLY VAL VAL HIS ARG          
SEQRES  11 B  325  ASP LEU LYS PRO GLU ASN LEU LEU PHE THR ASP GLU ASN          
SEQRES  12 B  325  ASP ASN LEU GLU ILE LYS ILE ILE ASP PHE GLY PHE ALA          
SEQRES  13 B  325  ARG LEU LYS PRO PRO ASP ASN GLN PRO LEU LYS THR PRO          
SEQRES  14 B  325  CYS PHE THR LEU HIS TYR ALA ALA PRO GLU LEU LEU ASN          
SEQRES  15 B  325  GLN ASN GLY TYR ASP GLU SER CYS ASP LEU TRP SER LEU          
SEQRES  16 B  325  GLY VAL ILE LEU TYR THR MET LEU SER GLY GLN VAL PRO          
SEQRES  17 B  325  PHE GLN SER HIS ASP ARG SER LEU THR CYS THR SER ALA          
SEQRES  18 B  325  VAL GLU ILE MET LYS LYS ILE LYS LYS GLY ASP PHE SER          
SEQRES  19 B  325  PHE GLU GLY GLU ALA TRP LYS ASN VAL SER GLN GLU ALA          
SEQRES  20 B  325  LYS ASP LEU ILE GLN GLY LEU LEU THR VAL ASP PRO ASN          
SEQRES  21 B  325  LYS ARG LEU LYS MET SER GLY LEU ARG TYR ASN GLU TRP          
SEQRES  22 B  325  LEU GLN ASP GLY SER GLN LEU SER SER ASN PRO LEU MET          
SEQRES  23 B  325  THR PRO ASP ILE LEU GLY SER SER GLY ALA ALA VAL HIS          
SEQRES  24 B  325  THR CYS VAL LYS ALA THR PHE HIS ALA PHE ASN LYS TYR          
SEQRES  25 B  325  LYS ARG GLU GLY PHE CYS LEU GLN ASN VAL ASP LYS ALA          
HET    ANP  A 400      31                                                       
HET    ANP  B 400      31                                                       
HETNAM     ANP PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER                      
FORMUL   3  ANP    2(C10 H17 N6 O12 P3)                                         
FORMUL   5  HOH   *84(H2 O)                                                     
HELIX    1   1 MET A  461  CYS A  475  1                                  15    
HELIX    2   2 GLU A  505  LYS A  513  1                                   9    
HELIX    3   3 SER A  517  VAL A  538  1                                  22    
HELIX    4   4 LYS A  546  GLU A  548  5                                   3    
HELIX    5   5 ASP A  600  GLY A  618  1                                  19    
HELIX    6   6 SER A  633  GLY A  644  1                                  12    
HELIX    7   7 GLY A  650  ASN A  655  1                                   6    
HELIX    8   8 SER A  657  THR A  669  1                                  13    
HELIX    9   9 ASN A  684  GLN A  688  5                                   5    
HELIX   10  10 MET A  699  SER A  706  1                                   8    
HELIX   11  11 SER A  707  ARG A  727  1                                  21    
HELIX   12  12 SER B  417  HIS B  422  1                                   6    
HELIX   13  13 MET B  461  CYS B  475  1                                  15    
HELIX   14  14 GLU B  505  LYS B  512  1                                   8    
HELIX   15  15 SER B  517  VAL B  538  1                                  22    
HELIX   16  16 LYS B  546  GLU B  548  5                                   3    
HELIX   17  17 GLU B  601  GLY B  618  1                                  18    
HELIX   18  18 SER B  633  GLY B  644  1                                  12    
HELIX   19  19 SER B  657  THR B  669  1                                  13    
HELIX   20  20 LYS B  677  ARG B  682  1                                   6    
HELIX   21  21 TYR B  683  GLN B  688  5                                   6    
HELIX   22  22 MET B  699  GLU B  728  1                                  30    
SHEET    1   A 3 TYR A 423  LEU A 425  0                                        
SHEET    2   A 3 SER A 438  HIS A 445 -1  O  VAL A 444   N  ASP A 424           
SHEET    3   A 3 GLY A 433  GLY A 435 -1  N  GLY A 433   O  CYS A 440           
SHEET    1   B 5 TYR A 423  LEU A 425  0                                        
SHEET    2   B 5 SER A 438  HIS A 445 -1  O  VAL A 444   N  ASP A 424           
SHEET    3   B 5 ALA A 451  SER A 458 -1  O  PHE A 452   N  CYS A 443           
SHEET    4   B 5 HIS A 493  GLU A 499 -1  O  THR A 494   N  ILE A 457           
SHEET    5   B 5 LEU A 484  HIS A 489 -1  N  PHE A 488   O  PHE A 495           
SHEET    1   C 2 VAL A 540  VAL A 541  0                                        
SHEET    2   C 2 ARG A 570  LEU A 571 -1  O  ARG A 570   N  VAL A 541           
SHEET    1   D 2 LEU A 550  PHE A 552  0                                        
SHEET    2   D 2 ILE A 561  ILE A 563 -1  O  LYS A 562   N  LEU A 551           
SHEET    1   E 5 TYR B 423  LEU B 425  0                                        
SHEET    2   E 5 SER B 438  HIS B 445 -1  O  VAL B 444   N  ASP B 424           
SHEET    3   E 5 GLN B 450  SER B 458 -1  O  VAL B 454   N  ARG B 441           
SHEET    4   E 5 HIS B 493  GLU B 499 -1  O  MET B 498   N  ALA B 453           
SHEET    5   E 5 LEU B 484  HIS B 489 -1  N  PHE B 488   O  PHE B 495           
SHEET    1   F 2 VAL B 540  VAL B 541  0                                        
SHEET    2   F 2 ARG B 570  LEU B 571 -1  O  ARG B 570   N  VAL B 541           
SHEET    1   G 2 LEU B 550  PHE B 552  0                                        
SHEET    2   G 2 ILE B 561  ILE B 563 -1  O  LYS B 562   N  LEU B 551           
SSBOND   1 CYS A  631    CYS A  714                          1555   1555  2.05  
SSBOND   2 CYS B  631    CYS B  714                          1555   1555  2.06  
CISPEP   1 SER A  679    GLY A  680          0         5.22                     
CISPEP   2 ARG A  727    GLU A  728          0       -13.67                     
CISPEP   3 GLU A  728    GLY A  729          0        -1.51                     
CISPEP   4 VAL B  670    ASP B  671          0        -7.86                     
CISPEP   5 ASP B  671    PRO B  672          0         0.56                     
CISPEP   6 ASN B  673    LYS B  674          0       -14.92                     
CISPEP   7 GLU B  728    GLY B  729          0        -2.02                     
SITE     1 AC1 13 HOH A  66  LEU A 432  GLY A 433  GLU A 434                    
SITE     2 AC1 13 GLU A 499  LEU A 500  LEU A 501  GLU A 505                    
SITE     3 AC1 13 GLU A 548  LEU A 551  ILE A 564  LYS A 643                    
SITE     4 AC1 13 LYS A 716                                                     
SITE     1 AC2 11 HOH B  76  LEU B 432  GLY B 433  GLU B 434                    
SITE     2 AC2 11 GLU B 499  LEU B 500  LEU B 501  GLU B 505                    
SITE     3 AC2 11 GLU B 548  LEU B 551  ILE B 564                               
CRYST1   51.561   91.250  135.460  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      0.019395  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010959  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007382        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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