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Database: PDB
Entry: 4XP2
LinkDB: 4XP2
Original site: 4XP2 
HEADER    TRANSFERASE                             16-JAN-15   4XP2              
TITLE     CRYSTAL STRUCTURE OF ERK2 IN COMPLEX WITH AN INHIBITOR                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MITOGEN-ACTIVATED PROTEIN KINASE 1;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: MAPK 1,ERT1,EXTRACELLULAR SIGNAL-REGULATED KINASE 2,ERK-2,  
COMPND   5 MAP KINASE ISOFORM P42,P42-MAPK,MITOGEN-ACTIVATED PROTEIN KINASE 2,  
COMPND   6 MAPK 2;                                                              
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                                         
KEYWDS    SERINE/THREONINE-PROTEIN KINASE, TRANSFERASE                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.GELIN,F.ALLEMAND,G.LABESSE,J.F.GUICHOU                              
REVDAT   3   06-SEP-17 4XP2    1       REMARK                                   
REVDAT   2   19-AUG-15 4XP2    1       JRNL                                     
REVDAT   1   12-AUG-15 4XP2    0                                                
JRNL        AUTH   M.GELIN,V.DELFOSSE,F.ALLEMAND,F.HOH,Y.SALLAZ-DAMAZ,          
JRNL        AUTH 2 M.PIROCCHI,W.BOURGUET,J.L.FERRER,G.LABESSE,J.F.GUICHOU       
JRNL        TITL   COMBINING `DRY' CO-CRYSTALLIZATION AND IN SITU DIFFRACTION   
JRNL        TITL 2 TO FACILITATE LIGAND SCREENING BY X-RAY CRYSTALLOGRAPHY.     
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  71  1777 2015              
JRNL        REFN                   ESSN 1399-0047                               
JRNL        PMID   26249358                                                     
JRNL        DOI    10.1107/S1399004715010342                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.75 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.6.4_486                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.75                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.30                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.120                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 67.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 50815                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.187                           
REMARK   3   R VALUE            (WORKING SET) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.930                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2503                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 28.2991 -  4.5750    0.65     2622   126  0.1788 0.2085        
REMARK   3     2  4.5750 -  3.6337    0.61     2429   138  0.1412 0.1543        
REMARK   3     3  3.6337 -  3.1751    0.63     2511   122  0.1682 0.2057        
REMARK   3     4  3.1751 -  2.8851    0.65     2619   129  0.1766 0.2112        
REMARK   3     5  2.8851 -  2.6785    0.64     2580   146  0.1771 0.2291        
REMARK   3     6  2.6785 -  2.5207    0.66     2628   156  0.1722 0.2333        
REMARK   3     7  2.5207 -  2.3945    0.67     2708   147  0.1711 0.2335        
REMARK   3     8  2.3945 -  2.2903    0.68     2701   164  0.1732 0.2593        
REMARK   3     9  2.2903 -  2.2022    0.68     2684   127  0.1879 0.2220        
REMARK   3    10  2.2022 -  2.1262    0.68     2719   167  0.1746 0.2438        
REMARK   3    11  2.1262 -  2.0597    0.68     2727   162  0.1946 0.2212        
REMARK   3    12  2.0597 -  2.0009    0.69     2777   121  0.1963 0.2551        
REMARK   3    13  2.0009 -  1.9482    0.69     2762   133  0.2181 0.2959        
REMARK   3    14  1.9482 -  1.9007    0.69     2774   143  0.2473 0.3448        
REMARK   3    15  1.9007 -  1.8575    0.70     2788   128  0.2681 0.3211        
REMARK   3    16  1.8575 -  1.8180    0.69     2787   119  0.2870 0.3364        
REMARK   3    17  1.8180 -  1.7816    0.70     2839   148  0.3395 0.3704        
REMARK   3    18  1.7816 -  1.7480    0.66     2657   127  0.3755 0.3860        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.35                                          
REMARK   3   B_SOL              : 53.96                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.270            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.500           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.64                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.30770                                             
REMARK   3    B22 (A**2) : 2.21580                                              
REMARK   3    B33 (A**2) : -1.90820                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.08870                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           2933                                  
REMARK   3   ANGLE     :  0.951           3970                                  
REMARK   3   CHIRALITY :  0.064            435                                  
REMARK   3   PLANARITY :  0.004            502                                  
REMARK   3   DIHEDRAL  : 13.640           1133                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 9:118)                              
REMARK   3    ORIGIN FOR THE GROUP (A): -13.6207  12.2774  34.1932              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2668 T22:   0.1891                                     
REMARK   3      T33:   0.1372 T12:  -0.0046                                     
REMARK   3      T13:  -0.0428 T23:   0.0571                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5514 L22:   0.2166                                     
REMARK   3      L33:   1.8662 L12:   0.3002                                     
REMARK   3      L13:   0.0572 L23:   0.3973                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1093 S12:   0.1756 S13:   0.1235                       
REMARK   3      S21:  -0.2172 S22:   0.1422 S23:   0.0795                       
REMARK   3      S31:  -0.3980 S32:  -0.2020 S33:  -0.0055                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 119:312)                            
REMARK   3    ORIGIN FOR THE GROUP (A):   1.2067   7.9098  57.3453              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1044 T22:   0.1115                                     
REMARK   3      T33:   0.1411 T12:   0.0069                                     
REMARK   3      T13:   0.0094 T23:   0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7758 L22:   0.4781                                     
REMARK   3      L33:   0.9734 L12:   0.5546                                     
REMARK   3      L13:   0.6146 L23:   0.3147                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0041 S12:   0.0019 S13:   0.0486                       
REMARK   3      S21:   0.0264 S22:   0.0206 S23:   0.0066                       
REMARK   3      S31:   0.0096 S32:   0.0506 S33:  -0.0244                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 313:354)                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.3320  -0.6371  35.5849              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1961 T22:   0.2413                                     
REMARK   3      T33:   0.1628 T12:  -0.0343                                     
REMARK   3      T13:   0.0295 T23:  -0.0320                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5162 L22:   0.7708                                     
REMARK   3      L33:   1.2497 L12:   0.0043                                     
REMARK   3      L13:   0.7647 L23:  -0.1152                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0292 S12:   0.2273 S13:  -0.0620                       
REMARK   3      S21:  -0.3013 S22:   0.0652 S23:  -0.0083                       
REMARK   3      S31:   0.3968 S32:   0.4825 S33:  -0.0700                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN S                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.0648   6.2991  51.0661              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1584 T22:   0.1586                                     
REMARK   3      T33:   0.1750 T12:  -0.0063                                     
REMARK   3      T13:   0.0103 T23:   0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1888 L22:   0.4415                                     
REMARK   3      L33:   0.6176 L12:  -0.0106                                     
REMARK   3      L13:   0.1730 L23:   0.1031                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0297 S12:  -0.0043 S13:  -0.0203                       
REMARK   3      S21:  -0.0224 S22:   0.0408 S23:  -0.0072                       
REMARK   3      S31:  -0.0206 S32:   0.0291 S33:  -0.0072                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A): -16.0153  13.7636  41.3115              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5817 T22:   0.6779                                     
REMARK   3      T33:   0.2131 T12:  -0.2131                                     
REMARK   3      T13:  -0.0260 T23:  -0.0192                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9849 L22:   5.2389                                     
REMARK   3      L33:   6.4828 L12:   6.4577                                     
REMARK   3      L13:   6.3376 L23:   4.9712                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0521 S12:   0.0295 S13:  -0.0623                       
REMARK   3      S21:  -0.1655 S22:   0.2680 S23:  -0.1623                       
REMARK   3      S31:  -0.0484 S32:  -0.1916 S33:  -0.1633                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4XP2 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-JAN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000205980.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-MAY-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM30A                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97970                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 69472                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.740                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 89.7                               
REMARK 200  DATA REDUNDANCY                : 1.800                              
REMARK 200  R MERGE                    (I) : 0.03500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.74                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.83                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 1.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.28900                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: 3QYW                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.37                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG MME 2000, 0.1M MES PH 6.5,       
REMARK 280  0.1M AMMONIUM SULFATE, 0.02M BETA-MERCAPTOETHANOL, VAPOR            
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291K                           
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       35.15700            
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.                         
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 TOTAL BURIED SURFACE AREA: 790 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 16200 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 KCAL/MOL                        
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     ASP A   330                                                      
REMARK 465     MET A   331                                                      
REMARK 465     GLU A   332                                                      
REMARK 465     LEU A   333                                                      
REMARK 465     ASP A   334                                                      
REMARK 465     ASP A   335                                                      
REMARK 465     LEU A   336                                                      
REMARK 465     PRO A   354                                                      
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     PHE A 329    CG   CD1  CD2  CE1  CE2  CZ                         
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       42.08   -142.93                                   
REMARK 500    ASP A 165       85.42     60.84                                   
REMARK 500    ASN A 199       19.44   -160.28                                   
REMARK 500    LEU A 292       47.92    -98.12                                   
REMARK 500    ASP A 316       94.20   -161.54                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 772        DISTANCE =  5.89 ANGSTROMS                       
REMARK 525    HOH A 773        DISTANCE =  5.97 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TT4 A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue DMS 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 SO4 A 405                 
DBREF  4XP2 A    8   358  UNP    P63086   MK01_RAT         8    358             
SEQRES   1 A  351  GLY PRO GLU MET VAL ARG GLY GLN VAL PHE ASP VAL GLY          
SEQRES   2 A  351  PRO ARG TYR THR ASN LEU SER TYR ILE GLY GLU GLY ALA          
SEQRES   3 A  351  TYR GLY MET VAL CYS SER ALA TYR ASP ASN LEU ASN LYS          
SEQRES   4 A  351  VAL ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU HIS          
SEQRES   5 A  351  GLN THR TYR CYS GLN ARG THR LEU ARG GLU ILE LYS ILE          
SEQRES   6 A  351  LEU LEU ARG PHE ARG HIS GLU ASN ILE ILE GLY ILE ASN          
SEQRES   7 A  351  ASP ILE ILE ARG ALA PRO THR ILE GLU GLN MET LYS ASP          
SEQRES   8 A  351  VAL TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU TYR          
SEQRES   9 A  351  LYS LEU LEU LYS THR GLN HIS LEU SER ASN ASP HIS ILE          
SEQRES  10 A  351  CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS TYR          
SEQRES  11 A  351  ILE HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  12 A  351  SER ASN LEU LEU LEU ASN THR THR CME ASP LEU LYS ILE          
SEQRES  13 A  351  CYS ASP PHE GLY LEU ALA ARG VAL ALA ASP PRO ASP HIS          
SEQRES  14 A  351  ASP HIS THR GLY PHE LEU THR GLU TYR VAL ALA THR ARG          
SEQRES  15 A  351  TRP TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS GLY          
SEQRES  16 A  351  TYR THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS ILE          
SEQRES  17 A  351  LEU ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO GLY          
SEQRES  18 A  351  LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY ILE          
SEQRES  19 A  351  LEU GLY SER PRO SER GLN GLU ASP LEU ASN CME ILE ILE          
SEQRES  20 A  351  ASN LEU LYS ALA ARG ASN TYR LEU LEU SER LEU PRO HIS          
SEQRES  21 A  351  LYS ASN LYS VAL PRO TRP ASN ARG LEU PHE PRO ASN ALA          
SEQRES  22 A  351  ASP SER LYS ALA LEU ASP LEU LEU ASP LYS MET LEU THR          
SEQRES  23 A  351  PHE ASN PRO HIS LYS ARG ILE GLU VAL GLU GLN ALA LEU          
SEQRES  24 A  351  ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO SER ASP          
SEQRES  25 A  351  GLU PRO ILE ALA GLU ALA PRO PHE LYS PHE ASP MET GLU          
SEQRES  26 A  351  LEU ASP ASP LEU PRO LYS GLU LYS LEU LYS GLU LEU ILE          
SEQRES  27 A  351  PHE GLU GLU THR ALA ARG PHE GLN PRO GLY TYR ARG SER          
MODRES 4XP2 CME A  159  CYS  MODIFIED RESIDUE                                   
MODRES 4XP2 CME A  252  CYS  MODIFIED RESIDUE                                   
HET    CME  A 159      10                                                       
HET    CME  A 252      10                                                       
HET    TT4  A 401      13                                                       
HET    DMS  A 402       4                                                       
HET    DMS  A 403       4                                                       
HET    SO4  A 404      10                                                       
HET    SO4  A 405       5                                                       
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     TT4 1-PHENYL-1H-1,2,4-TRIAZOLE-3,5-DIAMINE                           
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  CME    2(C5 H11 N O3 S2)                                            
FORMUL   2  TT4    C8 H9 N5                                                     
FORMUL   3  DMS    2(C2 H6 O S)                                                 
FORMUL   5  SO4    2(O4 S 2-)                                                   
FORMUL   7  HOH   *273(H2 O)                                                    
HELIX    1 AA1 HIS A   59  PHE A   76  1                                  18    
HELIX    2 AA2 LEU A  110  GLN A  117  1                                   8    
HELIX    3 AA3 SER A  120  ALA A  141  1                                  22    
HELIX    4 AA4 LYS A  149  SER A  151  5                                   3    
HELIX    5 AA5 ASP A  173  ASP A  177  5                                   5    
HELIX    6 AA6 THR A  188  ARG A  192  5                                   5    
HELIX    7 AA7 ALA A  193  ASN A  199  1                                   7    
HELIX    8 AA8 LYS A  205  ASN A  222  1                                  18    
HELIX    9 AA9 HIS A  230  GLY A  243  1                                  14    
HELIX   10 AB1 SER A  246  CME A  252  1                                   7    
HELIX   11 AB2 ASN A  255  LEU A  265  1                                  11    
HELIX   12 AB3 PRO A  272  PHE A  277  1                                   6    
HELIX   13 AB4 ASP A  281  LEU A  292  1                                  12    
HELIX   14 AB5 GLU A  301  ALA A  307  1                                   7    
HELIX   15 AB6 HIS A  308  GLU A  312  5                                   5    
HELIX   16 AB7 ASP A  316  GLU A  320  5                                   5    
HELIX   17 AB8 LYS A  338  THR A  349  1                                  12    
HELIX   18 AB9 ALA A  350  GLN A  353  5                                   4    
SHEET    1 AA1 2 MET A  11  VAL A  12  0                                        
SHEET    2 AA1 2 GLN A  15  VAL A  16 -1  O  GLN A  15   N  VAL A  12           
SHEET    1 AA2 5 TYR A  23  GLU A  31  0                                        
SHEET    2 AA2 5 MET A  36  ASP A  42 -1  O  TYR A  41   N  THR A  24           
SHEET    3 AA2 5 VAL A  47  ILE A  54 -1  O  VAL A  47   N  ASP A  42           
SHEET    4 AA2 5 VAL A  99  ASP A 104 -1  O  VAL A  99   N  ILE A  54           
SHEET    5 AA2 5 ASP A  86  ILE A  88 -1  N  ASP A  86   O  VAL A 102           
SHEET    1 AA3 3 THR A 108  ASP A 109  0                                        
SHEET    2 AA3 3 LEU A 153  LEU A 155 -1  O  LEU A 155   N  THR A 108           
SHEET    3 AA3 3 LEU A 161  ILE A 163 -1  O  LYS A 162   N  LEU A 154           
SHEET    1 AA4 2 VAL A 143  LEU A 144  0                                        
SHEET    2 AA4 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  1.33  
LINK         C   ASN A 251                 N   CME A 252     1555   1555  1.33  
LINK         C   CME A 252                 N   ILE A 253     1555   1555  1.33  
SITE     1 AC1  4 ALA A  50  GLN A 103  ASP A 104  MET A 106                    
SITE     1 AC2  6 LYS A 136  HIS A 139  SER A 140  LYS A 205                    
SITE     2 AC2  6 GLU A 303  HOH A 710                                          
SITE     1 AC3  4 HIS A 123  TYR A 126  ILE A 254  ARG A 259                    
SITE     1 AC4  7 TYR A 185  ARG A 189  ARG A 192  TYR A 231                    
SITE     2 AC4  7 HOH A 539  HOH A 603  HOH A 647                               
SITE     1 AC5  5 HIS A 297  LYS A 298  ARG A 299  ILE A 300                    
SITE     2 AC5  5 GLN A 304                                                     
CRYST1   48.637   70.314   59.827  90.00 108.93  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      0.020561  0.000000  0.007052        0.00000                         
SCALE2      0.000000  0.014222  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017671        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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