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Database: PDB
Entry: 4FV1
LinkDB: 4FV1
Original site: 4FV1 
HEADER    TRANSFERASE                             28-JUN-12   4FV1              
TITLE     CRYSTAL STRUCTURE OF THE ERK2 COMPLEXED WITH EK4                      
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 4FV1    1       AUTHOR                                   
REVDAT   1   22-AUG-12 4FV1    0                                                
JRNL        AUTH   Y.N.KANG,J.A.STUCKEY,X.XIE                                   
JRNL        TITL   CRYSTAL STRUCTURE OF THE ERK2 COMPLEXED WITH EK4             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.99 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) : 1.99                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 38.35                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 25723                          
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)  : 0.182                          
REMARK   3   R VALUE            (WORKING SET)  : 0.180                          
REMARK   3   FREE R VALUE                      : 0.225                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.080                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1307                           
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               : 13                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.99                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.07                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 97.82                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2563                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.1859                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2440                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.1839                   
REMARK   3   BIN FREE R VALUE                        : 0.2247                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.80                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 123                      
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            : 2772                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 59                                      
REMARK   3   SOLVENT ATOMS            : 213                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 28.93                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.12940                                              
REMARK   3    B22 (A**2) : -3.97240                                             
REMARK   3    B33 (A**2) : 1.84300                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 3.90910                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.217               
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) : 0.171               
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      : 0.938                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.907                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 2933   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 3986   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1342   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 69     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 455    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 2933   ; 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   : 373    ; 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   : 3516   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.009                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.91                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.89                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 2.81                     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: {A|9 - 107}                                            
REMARK   3    ORIGIN FOR THE GROUP (A):   18.1051    3.8975   25.1682           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0083 T22:    0.0121                                    
REMARK   3     T33:   -0.0409 T12:    0.0818                                    
REMARK   3     T13:   -0.0614 T23:   -0.0415                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   -0.4887 L22:    0.0476                                    
REMARK   3     L33:    2.4199 L12:    1.0914                                    
REMARK   3     L13:    0.2340 L23:    0.9998                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0015 S12:   -0.0021 S13:    0.0043                     
REMARK   3     S21:    0.0620 S22:    0.0251 S23:   -0.0154                     
REMARK   3     S31:   -0.0563 S32:    0.0466 S33:   -0.0266                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: {A|108 - 267}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):    4.0922    2.0232    2.3440           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0600 T22:   -0.0606                                    
REMARK   3     T33:   -0.0179 T12:   -0.0037                                    
REMARK   3     T13:    0.0194 T23:   -0.0165                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    1.6959 L22:    0.9546                                    
REMARK   3     L33:    1.3272 L12:   -0.8400                                    
REMARK   3     L13:    0.9349 L23:   -0.5281                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0434 S12:   -0.0481 S13:    0.0752                     
REMARK   3     S21:   -0.0017 S22:    0.0083 S23:   -0.0159                     
REMARK   3     S31:   -0.0176 S32:   -0.0384 S33:    0.0351                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: {A|268 - 275}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):    3.1167    4.9404  -16.0842           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0050 T22:    0.0157                                    
REMARK   3     T33:   -0.0119 T12:    0.0241                                    
REMARK   3     T13:    0.0080 T23:    0.0304                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.0320 L22:    0.0000                                    
REMARK   3     L33:    0.1375 L12:   -0.1100                                    
REMARK   3     L13:    0.0067 L23:   -0.0230                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0010 S12:   -0.0007 S13:   -0.0011                     
REMARK   3     S21:   -0.0051 S22:   -0.0072 S23:   -0.0062                     
REMARK   3     S31:   -0.0004 S32:   -0.0024 S33:    0.0082                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: {A|276 - 327}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):    9.3655   -9.0577   -3.0708           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0017 T22:   -0.0136                                    
REMARK   3     T33:   -0.0164 T12:    0.0054                                    
REMARK   3     T13:    0.0094 T23:   -0.0144                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.9820 L22:    1.2614                                    
REMARK   3     L33:    0.1744 L12:   -0.8524                                    
REMARK   3     L13:    0.4179 L23:   -0.4172                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:    0.0074 S12:    0.0429 S13:   -0.0282                     
REMARK   3     S21:   -0.0556 S22:   -0.0058 S23:    0.0101                     
REMARK   3     S31:    0.0436 S32:    0.0017 S33:   -0.0016                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: {A|328 - 354}                                          
REMARK   3    ORIGIN FOR THE GROUP (A):    5.7571   -1.5546   31.7077           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0237 T22:    0.0176                                    
REMARK   3     T33:   -0.0371 T12:    0.0133                                    
REMARK   3     T13:   -0.0489 T23:   -0.0420                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:   -0.1459 L22:    0.4329                                    
REMARK   3     L33:    0.4900 L12:   -0.0417                                    
REMARK   3     L13:    0.3218 L23:    0.8849                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0002 S12:   -0.0032 S13:   -0.0056                     
REMARK   3     S21:    0.0135 S22:    0.0032 S23:   -0.0028                     
REMARK   3     S31:    0.0115 S32:   -0.0227 S33:   -0.0030                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4FV1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-JUL-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB073390.                                      
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   : 25736                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.990                              
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     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.05200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 20.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 87.3                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.18500                            
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   (%): 47.27                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.33                     
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 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       35.03500            
REMARK 290   SMTRY3   2  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     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     PHE A   329                                                      
REMARK 465     ASP A   330                                                      
REMARK 465     MET A   331                                                      
REMARK 465     GLY A   355                                                      
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     TYR A  34    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A  46    CG   CD   CE   NZ                                   
REMARK 470     GLN A  64    CG   CD   OE1  NE2                                  
REMARK 470     GLU A 184    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 254    CG1  CG2  CD1                                       
REMARK 470     ASN A 279    CG   OD1  ND2                                       
REMARK 470     GLU A 332    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 334    CG   OD1  OD2                                       
REMARK 470     ASP A 335    CG   OD1  OD2                                       
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 147       43.41   -145.20                                   
REMARK 500    ASP A 165       89.28     58.68                                   
REMARK 500    ASN A 199       15.52   -159.37                                   
REMARK 500    LEU A 292       46.25    -94.27                                   
REMARK 500    ASP A 335       59.44   -104.64                                   
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 EK4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL 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 EDO A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 407                 
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: 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: 4FV4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ERK2 COMPLEXED WITH EK7                     
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  4FV1 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 4FV1 CME A  159  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
HET    CME  A 159      10                                                       
HET    EK4  A 401      51                                                       
HET    GOL  A 402       6                                                       
HET    SO4  A 403       5                                                       
HET    EDO  A 404       4                                                       
HET    EDO  A 405       4                                                       
HET    EDO  A 406       4                                                       
HET    EDO  A 407       4                                                       
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     EK4 N-[(1S)-2-HYDROXY-1-PHENYLETHYL]-4-{4-[3-                        
HETNAM   2 EK4  (TRIFLUOROMETHYL)PHENYL]-1H-PYRAZOL-5-YL}-1H-PYRROLE-           
HETNAM   3 EK4  2-CARBOXAMIDE                                                   
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  CME    C5 H11 N O3 S2                                               
FORMUL   2  EK4    C23 H19 F3 N4 O2                                             
FORMUL   3  GOL    C3 H8 O3                                                     
FORMUL   4  SO4    O4 S 2-                                                      
FORMUL   5  EDO    4(C2 H6 O2)                                                  
FORMUL   9  HOH   *213(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 ASP A  173  ASP A  177  5                                   5    
HELIX    6   6 THR A  188  ARG A  192  5                                   5    
HELIX    7   7 ALA A  193  ASN A  199  1                                   7    
HELIX    8   8 LYS A  205  ASN A  222  1                                  18    
HELIX    9   9 HIS A  230  GLY A  243  1                                  14    
HELIX   10  10 SER A  246  CYS A  252  1                                   7    
HELIX   11  11 ASN A  255  SER A  264  1                                  10    
HELIX   12  12 PRO A  272  PHE A  277  1                                   6    
HELIX   13  13 ASP A  281  LEU A  292  1                                  12    
HELIX   14  14 GLU A  301  ALA A  307  1                                   7    
HELIX   15  15 HIS A  308  GLU A  312  5                                   5    
HELIX   16  16 ASP A  316  GLU A  320  5                                   5    
HELIX   17  17 PRO A  337  THR A  349  1                                  13    
HELIX   18  18 ALA A  350  GLN A  353  5                                   4    
SHEET    1   A 5 TYR A  23  GLY A  32  0                                        
SHEET    2   A 5 GLY A  35  ASP A  42 -1  O  TYR A  41   N  THR A  24           
SHEET    3   A 5 VAL A  47  ILE A  54 -1  O  ILE A  51   N  CYS A  38           
SHEET    4   A 5 VAL A  99  GLN A 103 -1  O  VAL A  99   N  ILE A  54           
SHEET    5   A 5 ASP A  86  ILE A  88 -1  N  ILE A  88   O  TYR A 100           
SHEET    1   B 3 THR A 108  ASP A 109  0                                        
SHEET    2   B 3 LEU A 153  LEU A 155 -1  O  LEU A 155   N  THR A 108           
SHEET    3   B 3 LEU A 161  ILE A 163 -1  O  LYS A 162   N  LEU A 154           
SHEET    1   C 2 VAL A 143  LEU A 144  0                                        
SHEET    2   C 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  1.33  
LINK         C   CME A 159                 N   ASP A 160     1555   1555  1.35  
CISPEP   1 GLY A   20    PRO A   21          0         1.55                     
SITE     1 AC1 18 GLY A  30  TYR A  34  GLY A  35  VAL A  37                    
SITE     2 AC1 18 ALA A  50  LYS A  52  ILE A  82  GLN A 103                    
SITE     3 AC1 18 ASP A 104  MET A 106  ASP A 109  SER A 151                    
SITE     4 AC1 18 ASN A 152  LEU A 154  CYS A 164  ASP A 165                    
SITE     5 AC1 18 HOH A 518  HOH A 679                                          
SITE     1 AC2  8 GLU A  79  ASN A  80  TYR A 126  GLN A 130                    
SITE     2 AC2  8 ARG A 133  ASP A 160  HOH A 541  HOH A 675                    
SITE     1 AC3  5 TYR A 185  ARG A 189  ARG A 192  TYR A 231                    
SITE     2 AC3  5 HOH A 619                                                     
SITE     1 AC4  2 HIS A 118  ASN A 222                                          
SITE     1 AC5  5 ARG A  68  VAL A 171  PHE A 327  LEU A 333                    
SITE     2 AC5  5 HOH A 674                                                     
SITE     1 AC6  4 HIS A 297  LYS A 298  ARG A 299  GLN A 304                    
SITE     1 AC7  2 LYS A 149  SER A 151                                          
CRYST1   48.750   70.070   60.330  90.00 109.95  90.00 P 1 21 1      2          
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      0.020513  0.000000  0.007446        0.00000                         
SCALE2      0.000000  0.014271  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017634        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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