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Database: PDB
Entry: 3KN6
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Original site: 3KN6 
HEADER    TRANSFERASE                             12-NOV-09   3KN6              
TITLE     CRYSTAL STRUCTURE OF THE C-TERMINAL KINASE DOMAIN OF MSK1             
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 3KN6    1       JRNL                                     
REVDAT   2   12-MAY-10 3KN6    1       JRNL                                     
REVDAT   1   21-APR-10 3KN6    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.    2.00 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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.87                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.890                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 52.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 43443                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.219                           
REMARK   3   R VALUE            (WORKING SET) : 0.216                           
REMARK   3   FREE R VALUE                     : 0.263                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2183                            
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 45.8815 -  5.0440    0.57     2775   159  0.2251 0.2600        
REMARK   3     2  5.0440 -  4.0044    0.54     2673   129  0.1802 0.2426        
REMARK   3     3  4.0044 -  3.4984    0.53     2623   151  0.2022 0.2301        
REMARK   3     4  3.4984 -  3.1786    0.53     2616   143  0.2105 0.2533        
REMARK   3     5  3.1786 -  2.9508    0.53     2610   128  0.2262 0.2510        
REMARK   3     6  2.9508 -  2.7769    0.53     2575   145  0.2297 0.3182        
REMARK   3     7  2.7769 -  2.6378    0.53     2597   139  0.2285 0.2624        
REMARK   3     8  2.6378 -  2.5230    0.52     2559   153  0.2211 0.2541        
REMARK   3     9  2.5230 -  2.4259    0.52     2579   133  0.2110 0.2696        
REMARK   3    10  2.4259 -  2.3422    0.52     2570   120  0.2105 0.2652        
REMARK   3    11  2.3422 -  2.2689    0.52     2557   150  0.2214 0.2872        
REMARK   3    12  2.2689 -  2.2041    0.52     2550   123  0.2330 0.3077        
REMARK   3    13  2.2041 -  2.1461    0.52     2521   143  0.2157 0.2537        
REMARK   3    14  2.1461 -  2.0937    0.52     2592   127  0.2269 0.2848        
REMARK   3    15  2.0937 -  2.0461    0.51     2519   129  0.2287 0.3102        
REMARK   3    16  2.0461 -  2.0000    0.47     2344   111  0.2505 0.3245        
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              : 0.38                                          
REMARK   3   B_SOL              : 53.67                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.320            
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) : 33.23                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -6.49880                                             
REMARK   3    B22 (A**2) : 9.23910                                              
REMARK   3    B33 (A**2) : -2.74030                                             
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      :  0.005           4629                                  
REMARK   3   ANGLE     :  0.980           6212                                  
REMARK   3   CHIRALITY :  0.071            681                                  
REMARK   3   PLANARITY :  0.003            786                                  
REMARK   3   DIHEDRAL  : 18.544           1722                                  
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 3KN6 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-NOV-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB056200.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-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(111)                            
REMARK 200  OPTICS                         : MIRRORS                            
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   : 43534                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.870                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.09100                            
REMARK 200  R SYM                      (I) : 0.09100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 31.4000                            
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) : 2.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.44100                            
REMARK 200  R SYM FOR SHELL            (I) : 0.44100                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.100                              
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   (%): 42.76                                     
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       25.69300            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       67.47250            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       45.86950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       67.47250            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       25.69300            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       45.86950            
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     SER B   628                                                      
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 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     HIS B 625    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ASP B 626    CG   OD1  OD2                                       
REMARK 470     ARG B 627    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 629    CG   CD1  CD2                                       
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   SG   CYS A   631     CB   CYS A   714              2.00            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO B 672   C   -  N   -  CD  ANGL. DEV. = -17.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ARG A 543       -4.89     76.43                                   
REMARK 500    ASP A 544       38.95   -140.11                                   
REMARK 500    ASP A 565       79.38     61.90                                   
REMARK 500    TYR A 599       97.78    -68.72                                   
REMARK 500    PHE A 648       69.64   -116.28                                   
REMARK 500    ARG B 543       -1.20     73.92                                   
REMARK 500    ASP B 544       43.31   -143.96                                   
REMARK 500    ASP B 565       82.82     57.59                                   
REMARK 500    TYR B 599       97.07    -66.29                                   
REMARK 500    GLN B 623     -169.89   -106.03                                   
REMARK 500    PRO B 672      -51.92      0.34                                   
REMARK 500    ASN B 673       -7.82   -169.50                                   
REMARK 500    GLU B 728       67.70   -114.56                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 ASP B  671     PRO B  672                  -90.09                    
REMARK 500 ASN B  673     LYS B  674                 -146.96                    
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    THR A 700        24.7      L          L   OUTSIDE RANGE           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3KN5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE C-TERMINAL KINASE DOMAIN OF MSK1            
REMARK 900 IN COMPLEX WITH AMP-PNP                                              
DBREF  3KN6 A  414   738  UNP    O75582   KS6A5_HUMAN    414    738             
DBREF  3KN6 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          
FORMUL   3  HOH   *209(H2 O)                                                    
HELIX    1   1 SER A  417  HIS A  422  1                                   6    
HELIX    2   2 MET A  461  CYS A  475  1                                  15    
HELIX    3   3 GLU A  505  LYS A  513  1                                   9    
HELIX    4   4 SER A  517  VAL A  538  1                                  22    
HELIX    5   5 LYS A  546  GLU A  548  5                                   3    
HELIX    6   6 GLU A  601  GLY A  618  1                                  18    
HELIX    7   7 SER A  633  LYS A  642  1                                  10    
HELIX    8   8 GLY A  650  ASN A  655  1                                   6    
HELIX    9   9 SER A  657  THR A  669  1                                  13    
HELIX   10  10 ASN A  684  GLN A  688  5                                   5    
HELIX   11  11 MET A  699  GLY A  729  1                                  31    
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 LEU B  506  LYS B  513  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 GLY B  650  ASN B  655  1                                   6    
HELIX   20  20 SER B  657  THR B  669  1                                  13    
HELIX   21  21 LYS B  677  ARG B  682  1                                   6    
HELIX   22  22 TYR B  683  GLN B  688  5                                   6    
HELIX   23  23 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  ILE A 456   N  ILE A 439           
SHEET    4   B 5 HIS A 493  MET A 498 -1  O  MET A 498   N  ALA A 453           
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  THR A 553  0                                        
SHEET    2   D 2 GLU A 560  ILE A 563 -1  O  LYS A 562   N  LEU A 551           
SHEET    1   E 3 TYR B 423  LEU B 425  0                                        
SHEET    2   E 3 SER B 438  HIS B 445 -1  O  VAL B 444   N  ASP B 424           
SHEET    3   E 3 GLY B 433  GLY B 435 -1  N  GLY B 433   O  CYS B 440           
SHEET    1   F 5 TYR B 423  LEU B 425  0                                        
SHEET    2   F 5 SER B 438  HIS B 445 -1  O  VAL B 444   N  ASP B 424           
SHEET    3   F 5 ALA B 451  SER B 458 -1  O  ILE B 456   N  ILE B 439           
SHEET    4   F 5 HIS B 493  MET B 498 -1  O  MET B 498   N  ALA B 453           
SHEET    5   F 5 LEU B 484  HIS B 489 -1  N  GLU B 486   O  VAL B 497           
SHEET    1   G 3 GLY B 504  GLU B 505  0                                        
SHEET    2   G 3 LEU B 550  PHE B 552 -1  O  PHE B 552   N  GLY B 504           
SHEET    3   G 3 ILE B 561  ILE B 563 -1  O  LYS B 562   N  LEU B 551           
SHEET    1   H 2 VAL B 540  VAL B 541  0                                        
SHEET    2   H 2 ARG B 570  LEU B 571 -1  O  ARG B 570   N  VAL B 541           
SSBOND   1 CYS A  631    CYS A  714                          1555   1555  0.64  
SSBOND   2 CYS B  631    CYS B  714                          1555   1555  2.06  
CISPEP   1 MET A  678    SER A  679          0         0.62                     
CISPEP   2 VAL B  670    ASP B  671          0        -7.36                     
CISPEP   3 GLU B  728    GLY B  729          0        -0.42                     
CRYST1   51.386   91.739  134.945  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      0.019461  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010900  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007410        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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