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Database: PDB
Entry: 2Z7L
LinkDB: 2Z7L
Original site: 2Z7L 
HEADER    TRANSFERASE                             27-AUG-07   2Z7L              
TITLE     UNPHOSPHORYLATED MITOGEN ACTIVATED PROTEIN KINASE ERK2 IN             
TITLE    2 COMPLEX WITH (4-{[5-CARBAMOYL-4-(3-METHYLANILINO)PYRIMIDIN           
TITLE    3 2-YL]AMINO}PHENYL)ACETIC ACID                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: EXTRACELLULAR SIGNAL-REGULATED KINASE 2, ERK-2,             
COMPND   5 MITOGEN-ACTIVATED PROTEIN KINASE 2, MAP KINASE 2, MAPK 2,            
COMPND   6 P42-MAPK, ERT1;                                                      
COMPND   7 EC: 2.7.11.24;                                                       
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: MAPK1, ERK2, MAPK, PRKM1;                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28B                                    
KEYWDS    TRANSFERASE, SERINE/THREONINE-PROTEIN KINASE, ATP-BINDING,            
KEYWDS   2 CELL CYCLE, PHOSPHORYLATION, ACETYLATION, NUCLEOTIDE-BINDING         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.KATAYAMA,H.KURIHARA                                                 
REVDAT   3   24-FEB-09 2Z7L    1       VERSN                                    
REVDAT   2   11-NOV-08 2Z7L    1       JRNL                                     
REVDAT   1   12-AUG-08 2Z7L    0                                                
JRNL        AUTH   N.KATAYAMA,M.ORITA,T.YAMAGUCHI,H.HISAMICHI,                  
JRNL        AUTH 2 S.KUROMITSU,H.KURIHARA,H.SAKASHITA,Y.MATSUMOTO,              
JRNL        AUTH 3 S.FUJITA,T.NIIMI                                             
JRNL        TITL   IDENTIFICATION OF A KEY ELEMENT FOR                          
JRNL        TITL 2 HYDROGEN-BONDING PATTERNS BETWEEN PROTEIN KINASES            
JRNL        TITL 3 AND THEIR INHIBITORS                                         
JRNL        REF    PROTEINS                      V.  73   795 2008              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   18767165                                                     
JRNL        DOI    10.1002/PROT.22207                                           
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.41 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX 2002                                             
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN,ACCELRYS                   
REMARK   3               : SOFTWARE INC.(BADGER,BERARD,KUMAR,SZALMA,            
REMARK   3               : YIP,DZAKULA)                                         
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.41                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.31                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 397568.940                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 82.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 12380                          
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) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.223                           
REMARK   3   FREE R VALUE                     : 0.276                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.300                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1271                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008                           
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL                 
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 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       (A) : 2.40                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 49.30                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 1128                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2750                       
REMARK   3   BIN FREE R VALUE                    : 0.3310                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.00                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 125                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.030                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2690                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 45                                      
REMARK   3   SOLVENT ATOMS            : 129                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 33.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 40.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -5.53000                                             
REMARK   3    B22 (A**2) : 10.79000                                             
REMARK   3    B33 (A**2) : -5.26000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 3.21000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.29                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.28                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.39                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.37                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 21.60                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 2.70                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.250 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 2.030 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.830 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.650 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.36                                                 
REMARK   3   BSOL        : 60.13                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2Z7L COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 31-AUG-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB027621.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 06-JUN-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
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 RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00                               
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 : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12389                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.310                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.07700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: CNX 2002                                              
REMARK 200 STARTING MODEL: PDB ENTRY 3ERK                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.59                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG550 MME, ETHYLENE GLYCOL, BETA-       
REMARK 280  MERCAPTOETHANOL, PH7.0, VAPOR DIFFUSION, SITTING DROP               
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       34.98100            
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    -5                                                      
REMARK 465     ALA A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     HIS A     1                                                      
REMARK 465     HIS A     2                                                      
REMARK 465     MET A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     ALA A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     PRO A    11                                                      
REMARK 465     GLU A    12                                                      
REMARK 465     MET A    13                                                      
REMARK 465     VAL A    14                                                      
REMARK 465     ARG A    15                                                      
REMARK 465     GLY A    16                                                      
REMARK 465     GLN A    17                                                      
REMARK 465     GLY A    34                                                      
REMARK 465     ALA A    35                                                      
REMARK 465     TYR A    36                                                      
REMARK 465     LYS A   330                                                      
REMARK 465     PHE A   331                                                      
REMARK 465     ASP A   332                                                      
REMARK 465     MET A   333                                                      
REMARK 465     GLU A   334                                                      
REMARK 465     LEU A   335                                                      
REMARK 465     ASP A   336                                                      
REMARK 465     ASP A   337                                                      
REMARK 465     TYR A   358                                                      
REMARK 465     ARG A   359                                                      
REMARK 465     SER A   360                                                      
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    SER A  29      122.28    179.36                                   
REMARK 500    ILE A  31      -47.18   -132.03                                   
REMARK 500    SER A  57       49.23   -157.40                                   
REMARK 500    THR A  63       22.45    -70.74                                   
REMARK 500    TYR A  64       16.36   -152.09                                   
REMARK 500    LYS A  99      -82.87   -117.74                                   
REMARK 500    THR A 110     -168.04   -177.08                                   
REMARK 500    THR A 118      -29.86   -156.16                                   
REMARK 500    ASP A 149       33.77   -148.43                                   
REMARK 500    ASP A 167       86.62     66.29                                   
REMARK 500    ASP A 175       60.45   -150.94                                   
REMARK 500    HIS A 178       56.92   -118.61                                   
REMARK 500    LEU A 184       60.05     64.43                                   
REMARK 500    ALA A 189      150.05    -40.28                                   
REMARK 500    LEU A 200      -54.50   -122.98                                   
REMARK 500    ASN A 201        5.90   -162.93                                   
REMARK 500    ARG A 225      139.32   -173.23                                   
REMARK 500    PHE A 228       76.08   -117.22                                   
REMARK 500    TYR A 233      -72.45    -27.01                                   
REMARK 500    LEU A 294       66.99   -101.41                                   
REMARK 500    ASP A 318       89.34   -157.27                                   
REMARK 500    GLU A 341      -38.74   -157.44                                   
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 SO4 A 2100                
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE S91 A 1001                
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 2001                
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 2002                
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 2003                
DBREF  2Z7L A    3   360  UNP    P63086   MK01_RAT         1    358             
SEQADV 2Z7L MET A   -5  UNP  P63086              EXPRESSION TAG                 
SEQADV 2Z7L ALA A   -4  UNP  P63086              EXPRESSION TAG                 
SEQADV 2Z7L HIS A   -3  UNP  P63086              EXPRESSION TAG                 
SEQADV 2Z7L HIS A   -2  UNP  P63086              EXPRESSION TAG                 
SEQADV 2Z7L HIS A   -1  UNP  P63086              EXPRESSION TAG                 
SEQADV 2Z7L HIS A    0  UNP  P63086              EXPRESSION TAG                 
SEQADV 2Z7L HIS A    1  UNP  P63086              EXPRESSION TAG                 
SEQADV 2Z7L HIS A    2  UNP  P63086              EXPRESSION TAG                 
SEQRES   1 A  366  MET ALA HIS HIS HIS HIS HIS HIS MET ALA ALA ALA ALA          
SEQRES   2 A  366  ALA ALA GLY PRO GLU MET VAL ARG GLY GLN VAL PHE ASP          
SEQRES   3 A  366  VAL GLY PRO ARG TYR THR ASN LEU SER TYR ILE GLY GLU          
SEQRES   4 A  366  GLY ALA TYR GLY MET VAL CYS SER ALA TYR ASP ASN LEU          
SEQRES   5 A  366  ASN LYS VAL ARG VAL ALA ILE LYS LYS ILE SER PRO PHE          
SEQRES   6 A  366  GLU HIS GLN THR TYR CYS GLN ARG THR LEU ARG GLU ILE          
SEQRES   7 A  366  LYS ILE LEU LEU ARG PHE ARG HIS GLU ASN ILE ILE GLY          
SEQRES   8 A  366  ILE ASN ASP ILE ILE ARG ALA PRO THR ILE GLU GLN MET          
SEQRES   9 A  366  LYS ASP VAL TYR ILE VAL GLN ASP LEU MET GLU THR ASP          
SEQRES  10 A  366  LEU TYR LYS LEU LEU LYS THR GLN HIS LEU SER ASN ASP          
SEQRES  11 A  366  HIS ILE CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU          
SEQRES  12 A  366  LYS TYR ILE HIS SER ALA ASN VAL LEU HIS ARG ASP LEU          
SEQRES  13 A  366  LYS PRO SER ASN LEU LEU LEU ASN THR THR CYS ASP LEU          
SEQRES  14 A  366  LYS ILE CYS ASP PHE GLY LEU ALA ARG VAL ALA ASP PRO          
SEQRES  15 A  366  ASP HIS ASP HIS THR GLY PHE LEU THR GLU TYR VAL ALA          
SEQRES  16 A  366  THR ARG TRP TYR ARG ALA PRO GLU ILE MET LEU ASN SER          
SEQRES  17 A  366  LYS GLY TYR THR LYS SER ILE ASP ILE TRP SER VAL GLY          
SEQRES  18 A  366  CYS ILE LEU ALA GLU MET LEU SER ASN ARG PRO ILE PHE          
SEQRES  19 A  366  PRO GLY LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU          
SEQRES  20 A  366  GLY ILE LEU GLY SER PRO SER GLN GLU ASP LEU ASN CYS          
SEQRES  21 A  366  ILE ILE ASN LEU LYS ALA ARG ASN TYR LEU LEU SER LEU          
SEQRES  22 A  366  PRO HIS LYS ASN LYS VAL PRO TRP ASN ARG LEU PHE PRO          
SEQRES  23 A  366  ASN ALA ASP SER LYS ALA LEU ASP LEU LEU ASP LYS MET          
SEQRES  24 A  366  LEU THR PHE ASN PRO HIS LYS ARG ILE GLU VAL GLU GLN          
SEQRES  25 A  366  ALA LEU ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO          
SEQRES  26 A  366  SER ASP GLU PRO ILE ALA GLU ALA PRO PHE LYS PHE ASP          
SEQRES  27 A  366  MET GLU LEU ASP ASP LEU PRO LYS GLU LYS LEU LYS GLU          
SEQRES  28 A  366  LEU ILE PHE GLU GLU THR ALA ARG PHE GLN PRO GLY TYR          
SEQRES  29 A  366  ARG SER                                                      
HET    SO4  A2100       5                                                       
HET    S91  A1001      28                                                       
HET    BME  A2001       4                                                       
HET    BME  A2002       4                                                       
HET    BME  A2003       4                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     S91 [4-({5-(AMINOCARBONYL)-4-[(3-METHYLPHENYL)                       
HETNAM   2 S91  AMINO]PYRIMIDIN-2-YL}AMINO)PHENYL]ACETIC ACID                   
HETNAM     BME BETA-MERCAPTOETHANOL                                             
HETSYN     S91 (4-{[5-CARBAMOYL-4-(3-METHYLANILINO)PYRIMIDIN-2-                 
HETSYN   2 S91  YL]AMINO}PHENYL)ACETIC ACID                                     
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3  S91    C20 H19 N5 O3                                                
FORMUL   4  BME    3(C2 H6 O S)                                                 
FORMUL   7  HOH   *129(H2 O)                                                    
HELIX    1   1 SER A   57  TYR A   64  5                                   8    
HELIX    2   2 CYS A   65  PHE A   78  1                                  14    
HELIX    3   3 LEU A  112  LYS A  117  1                                   6    
HELIX    4   4 SER A  122  ALA A  143  1                                  22    
HELIX    5   5 LYS A  151  SER A  153  5                                   3    
HELIX    6   6 ASP A  175  ASP A  179  5                                   5    
HELIX    7   7 THR A  190  ARG A  194  5                                   5    
HELIX    8   8 ALA A  195  MET A  199  5                                   5    
HELIX    9   9 LYS A  207  ASN A  224  1                                  18    
HELIX   10  10 HIS A  232  GLY A  245  1                                  14    
HELIX   11  11 SER A  248  ILE A  255  1                                   8    
HELIX   12  12 ASN A  257  LEU A  267  1                                  11    
HELIX   13  13 PRO A  274  PHE A  279  1                                   6    
HELIX   14  14 ASP A  283  LEU A  294  1                                  12    
HELIX   15  15 ASN A  297  ARG A  301  5                                   5    
HELIX   16  16 GLU A  303  ALA A  309  1                                   7    
HELIX   17  17 HIS A  310  GLU A  314  5                                   5    
HELIX   18  18 ASP A  318  GLU A  322  5                                   5    
HELIX   19  19 GLU A  341  THR A  351  1                                  11    
SHEET    1   A 3 TYR A  25  THR A  26  0                                        
SHEET    2   A 3 MET A  38  ASP A  44 -1  O  TYR A  43   N  THR A  26           
SHEET    3   A 3 TYR A  30  GLY A  32 -1  N  ILE A  31   O  VAL A  39           
SHEET    1   B 5 TYR A  25  THR A  26  0                                        
SHEET    2   B 5 MET A  38  ASP A  44 -1  O  TYR A  43   N  THR A  26           
SHEET    3   B 5 VAL A  49  ILE A  56 -1  O  LYS A  55   N  MET A  38           
SHEET    4   B 5 VAL A 101  ASP A 106 -1  O  VAL A 101   N  ILE A  56           
SHEET    5   B 5 ASP A  88  ILE A  90 -1  N  ASP A  88   O  VAL A 104           
SHEET    1   C 3 THR A 110  ASP A 111  0                                        
SHEET    2   C 3 LEU A 155  LEU A 157 -1  O  LEU A 157   N  THR A 110           
SHEET    3   C 3 LEU A 163  ILE A 165 -1  O  LYS A 164   N  LEU A 156           
SHEET    1   D 2 VAL A 145  LEU A 146  0                                        
SHEET    2   D 2 ARG A 172  VAL A 173 -1  O  ARG A 172   N  LEU A 146           
LINK         SG  CYS A 161                 S2  BME A2001     1555   1555  2.03  
LINK         SG  CYS A 254                 S2  BME A2002     1555   1555  2.03  
LINK         SG  CYS A 166                 S2  BME A2003     1555   1555  2.04  
SITE     1 AC1  3 ARG A 191  ARG A 194  TYR A 233                               
SITE     1 AC2 10 ILE A  31  GLY A  32  LYS A  54  GLN A 105                    
SITE     2 AC2 10 ASP A 106  MET A 108  THR A 110  ASP A 111                    
SITE     3 AC2 10 LYS A 114  LEU A 156                                          
SITE     1 AC3  6 PHE A 129  ASN A 158  THR A 159  CYS A 161                    
SITE     2 AC3  6 LEU A 258  HOH A2222                                          
SITE     1 AC4  3 CYS A 254  ASN A 297  HIS A 299                               
SITE     1 AC5  4 SER A 153  ASN A 154  CYS A 166  ASP A 167                    
CRYST1   48.873   69.962   60.775  90.00 109.58  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      0.020461  0.000000  0.007276        0.00000                         
SCALE2      0.000000  0.014294  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017464        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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