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Database: PDB
Entry: 4FV4
LinkDB: 4FV4
Original site: 4FV4 
HEADER    TRANSFERASE                             29-JUN-12   4FV4              
TITLE     CRYSTAL STRUCTURE OF THE ERK2 COMPLEXED WITH EK7                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MAP KINASE 1, MAPK 1, ERT1, EXTRACELLULAR SIGNAL-REGULATED  
COMPND   5 KINASE 2, ERK-2, MAP KINASE ISOFORM P42, P42-MAPK, MITOGEN-ACTIVATED 
COMPND   6 PROTEIN KINASE 2, MAP KINASE 2, MAPK 2;                              
COMPND   7 EC: 2.7.11.24;                                                       
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 STRAIN: HUMAN;                                                       
SOURCE   6 GENE: ERK2, MAPK1, PRKM1, PRKM2;                                     
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PT7BLUE                                   
KEYWDS    TRANSFERASE                                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.N.KANG,J.A.STUCKEY,X.XIE                                            
REVDAT   2   24-SEP-14 4FV4    1       AUTHOR                                   
REVDAT   1   29-AUG-12 4FV4    0                                                
JRNL        AUTH   Y.N.KANG,J.A.STUCKEY,X.XIE                                   
JRNL        TITL   CRYSTAL STRUCTURE OF THE ERK2 COMPLEXED WITH EK7             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.1                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 12881                          
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)  : 0.219                          
REMARK   3   R VALUE            (WORKING SET)  : 0.217                          
REMARK   3   FREE R VALUE                      : 0.253                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.950                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 637                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 6                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.50                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.74                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 94.94                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 3030                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2571                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2890                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2550                   
REMARK   3   BIN FREE R VALUE                        : 0.2970                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.62                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 140                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2626                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 47                                      
REMARK   3   SOLVENT ATOMS            : 42                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 37.48                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.31740                                             
REMARK   3    B22 (A**2) : 2.97980                                              
REMARK   3    B33 (A**2) : -0.66240                                             
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.361               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.657               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.917                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.879                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2760   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3760   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1264   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 67     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 425    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2760   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 357    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 3024   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.99                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.32                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 2.83                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: {A|7 - 106}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -12.1752    5.0208    5.8789           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0586 T22:    0.0299                                    
REMARK   3     T33:   -0.0080 T12:   -0.0103                                    
REMARK   3     T13:   -0.0291 T23:    0.0470                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.6434 L22:    0.3793                                    
REMARK   3     L33:    1.4567 L12:    0.3929                                    
REMARK   3     L13:    0.1804 L23:   -0.4658                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0016 S12:   -0.0048 S13:    0.0158                     
REMARK   3     S21:    0.0047 S22:    0.0096 S23:    0.0221                     
REMARK   3     S31:    0.0000 S32:    0.0112 S33:   -0.0080                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: {A|107 - 222}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -10.0192   -5.8511   24.7150           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0016 T22:   -0.0664                                    
REMARK   3     T33:    0.0078 T12:   -0.0016                                    
REMARK   3     T13:    0.0427 T23:    0.0217                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0372 L22:    1.3159                                    
REMARK   3     L33:    1.2738 L12:   -0.4051                                    
REMARK   3     L13:    0.2334 L23:   -0.5530                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0062 S12:    0.0060 S13:   -0.0007                     
REMARK   3     S21:   -0.0040 S22:    0.0031 S23:    0.0158                     
REMARK   3     S31:    0.0057 S32:    0.0114 S33:   -0.0093                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: {A|223 - 329}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):   -2.4197   -9.3402   34.8354           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0023 T22:   -0.0446                                    
REMARK   3     T33:    0.0063 T12:   -0.0328                                    
REMARK   3     T13:    0.0367 T23:   -0.0100                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0793 L22:    0.8903                                    
REMARK   3     L33:    0.6887 L12:    0.2243                                    
REMARK   3     L13:    0.5790 L23:    0.1171                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0095 S12:   -0.0438 S13:    0.0010                     
REMARK   3     S21:   -0.0325 S22:   -0.0268 S23:   -0.0050                     
REMARK   3     S31:    0.0339 S32:    0.0435 S33:    0.0173                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: {A|330 - 355}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):    2.0826    1.9693   -0.1442           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0064 T22:    0.0218                                    
REMARK   3     T33:   -0.0011 T12:   -0.0043                                    
REMARK   3     T13:   -0.0181 T23:    0.0141                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0696 L22:    0.2718                                    
REMARK   3     L33:    0.0000 L12:    0.3226                                    
REMARK   3     L13:   -0.1057 L23:   -0.2335                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0000 S12:   -0.0013 S13:   -0.0039                     
REMARK   3     S21:   -0.0114 S22:   -0.0032 S23:   -0.0036                     
REMARK   3     S31:    0.0039 S32:    0.0074 S33:    0.0032                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4FV4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-JUL-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB073393.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU                             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IIC                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12897                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 55.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 94.8                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.57                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.42500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 45.36                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM MES BUFFER, PH 6.5, 26-28% PEG-   
REMARK 280  MME 2000, 200 MM AMMONIUM SULFATE AND 20 MM 2-MERCAPTOETHANOL,      
REMARK 280  VAPOR DIFFUSION, TEMPERATURE 298K                                   
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       22.09500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       60.04500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.22500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       60.04500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       22.09500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.22500            
REMARK 290   SMTRY3   4  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     MET A    -1                                                      
REMARK 465     ALA A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     ALA A    33                                                      
REMARK 465     TYR A    34                                                      
REMARK 465     PRO A   174                                                      
REMARK 465     ASP A   175                                                      
REMARK 465     HIS A   176                                                      
REMARK 465     ASP A   177                                                      
REMARK 465     HIS A   178                                                      
REMARK 465     THR A   179                                                      
REMARK 465     GLY A   180                                                      
REMARK 465     PHE A   181                                                      
REMARK 465     LEU A   182                                                      
REMARK 465     THR A   183                                                      
REMARK 465     GLU A   184                                                      
REMARK 465     TYR A   185                                                      
REMARK 465     LEU A   198                                                      
REMARK 465     ASN A   199                                                      
REMARK 465     SER A   200                                                      
REMARK 465     LYS A   201                                                      
REMARK 465     GLY A   202                                                      
REMARK 465     TYR A   356                                                      
REMARK 465     ARG A   357                                                      
REMARK 465     SER A   358                                                      
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     VAL A  16    CG1  CG2                                            
REMARK 470     LYS A  46    CG   CD   CE   NZ                                   
REMARK 470     GLN A  60    CG   CD   OE1  NE2                                  
REMARK 470     LYS A  97    CG   CD   CE   NZ                                   
REMARK 470     LYS A 115    CG   CD   CE   NZ                                   
REMARK 470     TYR A 203    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TYR A 231    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN A 247    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 248    CG   CD   OE1  OE2                                  
REMARK 470     LEU A 250    CG   CD1  CD2                                       
REMARK 470     ASN A 251    CG   OD1  ND2                                       
REMARK 470     ILE A 253    CG1  CG2  CD1                                       
REMARK 470     LYS A 257    CG   CD   CE   NZ                                   
REMARK 470     ASP A 330    CG   OD1  OD2                                       
REMARK 470     GLU A 332    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 338    CG   CD   CE   NZ                                   
REMARK 470     GLU A 339    CG   CD   OE1  OE2                                  
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    VAL A  44      -60.54    -90.62                                   
REMARK 500    ARG A 146       -3.37     73.02                                   
REMARK 500    ASP A 147       43.84   -147.94                                   
REMARK 500    ASP A 165       86.85     63.88                                   
REMARK 500    ARG A 189      -51.69    -29.11                                   
REMARK 500    CYS A 252     -179.11   -173.02                                   
REMARK 500    LEU A 292       57.02    -93.01                                   
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 EK7 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 405                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4FUX   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ERK2 COMPLEXED WITH E75                     
REMARK 900 RELATED ID: 4FUY   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ERK2 COMPLEXED WITH EK2                     
REMARK 900 RELATED ID: 4FV0   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ERK2 COMPLEXED WITH EK3                     
REMARK 900 RELATED ID: 4FV1   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ERK2 COMPLEXED WITH EK4                     
REMARK 900 RELATED ID: 4FV2   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ERK2 COMPLEXED WITH EK5                     
REMARK 900 RELATED ID: 4FV3   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ERK2 COMPLEXED WITH EK6                     
REMARK 900 RELATED ID: 4FV5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ERK2 COMPLEXED WITH EK9                     
REMARK 900 RELATED ID: 4FV6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ERK2 COMPLEXED WITH E57                     
REMARK 900 RELATED ID: 4FV7   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ERK2 COMPLEXED WITH E94                     
REMARK 900 RELATED ID: 4FV8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ERK2 COMPLEXED WITH E63                     
REMARK 900 RELATED ID: 4FV9   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ERK2 COMPLEXED WITH E71                     
DBREF  4FV4 A   -1   358  UNP    P28482   MK01_HUMAN       1    360             
SEQRES   1 A  360  MET ALA ALA ALA ALA ALA ALA GLY ALA GLY PRO GLU MET          
SEQRES   2 A  360  VAL ARG GLY GLN VAL PHE ASP VAL GLY PRO ARG TYR THR          
SEQRES   3 A  360  ASN LEU SER TYR ILE GLY GLU GLY ALA TYR GLY MET VAL          
SEQRES   4 A  360  CYS SER ALA TYR ASP ASN VAL ASN LYS VAL ARG VAL ALA          
SEQRES   5 A  360  ILE LYS LYS ILE SER PRO PHE GLU HIS GLN THR TYR CYS          
SEQRES   6 A  360  GLN ARG THR LEU ARG GLU ILE LYS ILE LEU LEU ARG PHE          
SEQRES   7 A  360  ARG HIS GLU ASN ILE ILE GLY ILE ASN ASP ILE ILE ARG          
SEQRES   8 A  360  ALA PRO THR ILE GLU GLN MET LYS ASP VAL TYR ILE VAL          
SEQRES   9 A  360  GLN ASP LEU MET GLU THR ASP LEU TYR LYS LEU LEU LYS          
SEQRES  10 A  360  THR GLN HIS LEU SER ASN ASP HIS ILE CYS TYR PHE LEU          
SEQRES  11 A  360  TYR GLN ILE LEU ARG GLY LEU LYS TYR ILE HIS SER ALA          
SEQRES  12 A  360  ASN VAL LEU HIS ARG ASP LEU LYS PRO SER ASN LEU LEU          
SEQRES  13 A  360  LEU ASN THR THR CME ASP LEU LYS ILE CYS ASP PHE GLY          
SEQRES  14 A  360  LEU ALA ARG VAL ALA ASP PRO ASP HIS ASP HIS THR GLY          
SEQRES  15 A  360  PHE LEU THR GLU TYR VAL ALA THR ARG TRP TYR ARG ALA          
SEQRES  16 A  360  PRO GLU ILE MET LEU ASN SER LYS GLY TYR THR LYS SER          
SEQRES  17 A  360  ILE ASP ILE TRP SER VAL GLY CYS ILE LEU ALA GLU MET          
SEQRES  18 A  360  LEU SER ASN ARG PRO ILE PHE PRO GLY LYS HIS TYR LEU          
SEQRES  19 A  360  ASP GLN LEU ASN HIS ILE LEU GLY ILE LEU GLY SER PRO          
SEQRES  20 A  360  SER GLN GLU ASP LEU ASN CYS ILE ILE ASN LEU LYS ALA          
SEQRES  21 A  360  ARG ASN TYR LEU LEU SER LEU PRO HIS LYS ASN LYS VAL          
SEQRES  22 A  360  PRO TRP ASN ARG LEU PHE PRO ASN ALA ASP SER LYS ALA          
SEQRES  23 A  360  LEU ASP LEU LEU ASP LYS MET LEU THR PHE ASN PRO HIS          
SEQRES  24 A  360  LYS ARG ILE GLU VAL GLU GLN ALA LEU ALA HIS PRO TYR          
SEQRES  25 A  360  LEU GLU GLN TYR TYR ASP PRO SER ASP GLU PRO ILE ALA          
SEQRES  26 A  360  GLU ALA PRO PHE LYS PHE ASP MET GLU LEU ASP ASP LEU          
SEQRES  27 A  360  PRO LYS GLU LYS LEU LYS GLU LEU ILE PHE GLU GLU THR          
SEQRES  28 A  360  ALA ARG PHE GLN PRO GLY TYR ARG SER                          
MODRES 4FV4 CME A  159  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
HET    CME  A 159      10                                                       
HET    EK7  A 401      43                                                       
HET    SO4  A 402       5                                                       
HET    SO4  A 403       5                                                       
HET    SO4  A 404       5                                                       
HET    GOL  A 405       6                                                       
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     EK7 9-(DIMETHYLAMINO)-2-[(3-HYDROXYPHENYL)AMINO]-5,6-                
HETNAM   2 EK7  DIHYDROTHIENO[3,4-H]QUINAZOLINE-7-CARBONITRILE                  
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  CME    C5 H11 N O3 S2                                               
FORMUL   2  EK7    C19 H17 N5 O S                                               
FORMUL   3  SO4    3(O4 S 2-)                                                   
FORMUL   6  GOL    C3 H8 O3                                                     
FORMUL   7  HOH   *42(H2 O)                                                     
HELIX    1   1 HIS A   59  PHE A   76  1                                  18    
HELIX    2   2 LEU A  110  GLN A  117  1                                   8    
HELIX    3   3 SER A  120  ALA A  141  1                                  22    
HELIX    4   4 LYS A  149  SER A  151  5                                   3    
HELIX    5   5 THR A  188  ARG A  192  5                                   5    
HELIX    6   6 ALA A  193  MET A  197  5                                   5    
HELIX    7   7 LYS A  205  ASN A  222  1                                  18    
HELIX    8   8 HIS A  230  GLY A  243  1                                  14    
HELIX    9   9 SER A  246  ASN A  251  1                                   6    
HELIX   10  10 ASN A  255  LEU A  265  1                                  11    
HELIX   11  11 PRO A  272  PHE A  277  1                                   6    
HELIX   12  12 ASP A  281  LEU A  292  1                                  12    
HELIX   13  13 GLU A  301  ALA A  307  1                                   7    
HELIX   14  14 HIS A  308  GLU A  312  5                                   5    
HELIX   15  15 ASP A  316  GLU A  320  5                                   5    
HELIX   16  16 PRO A  337  ALA A  350  1                                  14    
HELIX   17  17 ARG A  351  GLN A  353  5                                   3    
SHEET    1   A 2 MET A  11  VAL A  12  0                                        
SHEET    2   A 2 GLN A  15  VAL A  16 -1  O  GLN A  15   N  VAL A  12           
SHEET    1   B 5 TYR A  23  GLY A  30  0                                        
SHEET    2   B 5 VAL A  37  ASP A  42 -1  O  TYR A  41   N  THR A  24           
SHEET    3   B 5 VAL A  47  ILE A  54 -1  O  VAL A  49   N  ALA A  40           
SHEET    4   B 5 VAL A  99  ASP A 104 -1  O  GLN A 103   N  ALA A  50           
SHEET    5   B 5 ASP A  86  ILE A  88 -1  N  ILE A  88   O  TYR A 100           
SHEET    1   C 3 THR A 108  ASP A 109  0                                        
SHEET    2   C 3 LEU A 153  LEU A 155 -1  O  LEU A 155   N  THR A 108           
SHEET    3   C 3 LEU A 161  ILE A 163 -1  O  LYS A 162   N  LEU A 154           
SHEET    1   D 2 VAL A 143  LEU A 144  0                                        
SHEET    2   D 2 ARG A 170  VAL A 171 -1  O  ARG A 170   N  LEU A 144           
LINK         C   THR A 158                 N   CME A 159     1555   1555  1.35  
LINK         C   CME A 159                 N   ASP A 160     1555   1555  1.35  
CISPEP   1 GLY A   20    PRO A   21          0         4.20                     
SITE     1 AC1 11 ILE A  29  ALA A  50  LYS A  52  GLN A 103                    
SITE     2 AC1 11 ASP A 104  MET A 106  GLU A 107  ASP A 109                    
SITE     3 AC1 11 LYS A 112  LEU A 154  ASP A 165                               
SITE     1 AC2  4 ARG A 189  ARG A 192  TYR A 231  GLN A 304                    
SITE     1 AC3  3 VAL A  12  SER A  27  TYR A  28                               
SITE     1 AC4  5 ARG A  65  ARG A  68  ARG A 146  LEU A 168                    
SITE     2 AC4  5 ARG A 170                                                     
SITE     1 AC5  3 HIS A  59  GLN A  60  THR A  61                               
CRYST1   44.190   70.450  120.090  90.00  90.00  90.00 P 21 21 21    4          
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      0.022630  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014194  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008327        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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