GenomeNet

Database: PDB
Entry: 4XP0
LinkDB: 4XP0
Original site: 4XP0 
HEADER    TRANSFERASE                             16-JAN-15   4XP0              
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: NORWAY 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 4XP0    1       REMARK SITE   ATOM                       
REVDAT   2   19-AUG-15 4XP0    1       JRNL                                     
REVDAT   1   12-AUG-15 4XP0    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.    1.46 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX                                               
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) : 1.46                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.63                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.310                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 82.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 64302                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.192                           
REMARK   3   R VALUE            (WORKING SET) : 0.190                           
REMARK   3   FREE R VALUE                     : 0.214                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5500                            
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 28.6365 -  4.5309    0.93     3944   197  0.1938 0.2182        
REMARK   3     2  4.5309 -  3.5985    0.92     3860   225  0.1459 0.1547        
REMARK   3     3  3.5985 -  3.1443    0.90     3829   176  0.1665 0.2157        
REMARK   3     4  3.1443 -  2.8571    0.89     3728   195  0.1681 0.1832        
REMARK   3     5  2.8571 -  2.6525    0.89     3746   213  0.1764 0.2051        
REMARK   3     6  2.6525 -  2.4962    0.88     3679   232  0.1716 0.1881        
REMARK   3     7  2.4962 -  2.3712    0.87     3626   213  0.1764 0.2296        
REMARK   3     8  2.3712 -  2.2681    0.86     3630   193  0.1812 0.2185        
REMARK   3     9  2.2681 -  2.1808    0.85     3553   216  0.1816 0.1796        
REMARK   3    10  2.1808 -  2.1055    0.86     3576   216  0.1697 0.1911        
REMARK   3    11  2.1055 -  2.0397    0.85     3547   175  0.1725 0.1964        
REMARK   3    12  2.0397 -  1.9814    0.84     3613   146  0.1827 0.1998        
REMARK   3    13  1.9814 -  1.9293    0.84     3525   199  0.1867 0.2382        
REMARK   3    14  1.9293 -  1.8822    0.83     3519   153  0.1982 0.2398        
REMARK   3    15  1.8822 -  1.8394    0.83     3521   162  0.1992 0.2159        
REMARK   3    16  1.8394 -  1.8003    0.83     3533   175  0.1992 0.2297        
REMARK   3    17  1.8003 -  1.7643    0.83     3498   156  0.2103 0.2157        
REMARK   3    18  1.7643 -  1.7310    0.82     3452   187  0.2186 0.2456        
REMARK   3    19  1.7310 -  1.7001    0.82     3433   189  0.2308 0.2400        
REMARK   3    20  1.7001 -  1.6713    0.81     3448   153  0.2449 0.2838        
REMARK   3    21  1.6713 -  1.6443    0.81     3382   193  0.2614 0.2955        
REMARK   3    22  1.6443 -  1.6190    0.80     3387   185  0.2818 0.3377        
REMARK   3    23  1.6190 -  1.5952    0.79     3340   183  0.2976 0.3243        
REMARK   3    24  1.5952 -  1.5728    0.80     3339   221  0.3125 0.3452        
REMARK   3    25  1.5728 -  1.5515    0.79     3355   168  0.3241 0.3563        
REMARK   3    26  1.5515 -  1.5314    0.79     3294   171  0.3409 0.3743        
REMARK   3    27  1.5314 -  1.5122    0.78     3349   156  0.3613 0.3561        
REMARK   3    28  1.5122 -  1.4940    0.76     3179   159  0.3846 0.4450        
REMARK   3    29  1.4940 -  1.4766    0.64     2702   156  0.3958 0.4194        
REMARK   3    30  1.4766 -  1.4600    0.58     2441   137  0.3937 0.3950        
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              : 64.31                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.320           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 19.29                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.85                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.43090                                             
REMARK   3    B22 (A**2) : 0.80240                                              
REMARK   3    B33 (A**2) : -0.37150                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.26970                                             
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      :  0.014           2989                                  
REMARK   3   ANGLE     :  1.100           4051                                  
REMARK   3   CHIRALITY :  0.076            454                                  
REMARK   3   PLANARITY :  0.006            508                                  
REMARK   3   DIHEDRAL  : 13.453           1174                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  -4.3706   5.6043  48.3292              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0659 T22:   0.0964                                     
REMARK   3      T33:   0.1017 T12:  -0.0035                                     
REMARK   3      T13:   0.0108 T23:   0.0267                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5986 L22:   0.3794                                     
REMARK   3      L33:   0.8474 L12:   0.2456                                     
REMARK   3      L13:   0.2897 L23:   0.2926                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0507 S12:   0.0735 S13:   0.0827                       
REMARK   3      S21:  -0.0643 S22:   0.0478 S23:  -0.0111                       
REMARK   3      S31:  -0.0770 S32:   0.0477 S33:  -0.0007                       
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 4XP0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 20-JAN-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000206003.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-NOV-11                          
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                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.872600                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA 3.2.19                       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 64331                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.460                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.631                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : 0.03100                            
REMARK 200  R SYM                      (I) : 0.03100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.46                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 85.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.48000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.48000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.19                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.42                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG MME 2000, 0.1M MES PH 6.5, 0.1M      
REMARK 280  AMMONIUM SULFATE, 0.02M BETA-MERCAPTOETHANOL, VAPOR DIFFUSION,      
REMARK 280  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       35.39500            
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: 530 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 16350 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 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     LYS A   328                                                      
REMARK 465     PHE A   329                                                      
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     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    CZ   OH                                             
REMARK 470     GLU A 184    OE1  OE2                                            
REMARK 470     ASP A 335    CB   CG   OD1  OD2                                  
REMARK 470     GLU A 339    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 147       41.37   -147.80                                   
REMARK 500    ASP A 165       87.23     63.35                                   
REMARK 500    ASN A 199       18.72   -160.46                                   
REMARK 500    LEU A 292       46.35    -98.62                                   
REMARK 500    ASP A 316       97.13   -160.52                                   
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 852        DISTANCE =  5.97 ANGSTROMS                       
REMARK 525    HOH A 853        DISTANCE =  6.14 ANGSTROMS                       
REMARK 525    HOH A 854        DISTANCE =  6.43 ANGSTROMS                       
REMARK 525    HOH A 855        DISTANCE =  7.20 ANGSTROMS                       
REMARK 525    HOH A 856        DISTANCE =  7.54 ANGSTROMS                       
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 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 42A A 404                 
DBREF  4XP0 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  CME 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  CME 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 4XP0 CME A  125  CYS  MODIFIED RESIDUE                                   
MODRES 4XP0 CME A  159  CYS  MODIFIED RESIDUE                                   
MODRES 4XP0 CME A  164  CYS  MODIFIED RESIDUE                                   
MODRES 4XP0 CME A  252  CYS  MODIFIED RESIDUE                                   
HET    CME  A 125      10                                                       
HET    CME  A 159      10                                                       
HET    CME  A 164      10                                                       
HET    CME  A 252      10                                                       
HET    SO4  A 401       5                                                       
HET    DMS  A 402       4                                                       
HET    DMS  A 403       4                                                       
HET    42A  A 404      11                                                       
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     SO4 SULFATE ION                                                      
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     42A 1H-PYRROLO[2,3-B]PYRIDINE-3-CARBONITRILE                         
FORMUL   1  CME    4(C5 H11 N O3 S2)                                            
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3  DMS    2(C2 H6 O S)                                                 
FORMUL   5  42A    C8 H5 N3                                                     
FORMUL   6  HOH   *356(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  MET A  197  5                                   5    
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 PRO A  337  ALA A  350  1                                  14    
HELIX   18 AB9 ARG A  351  GLN A  353  5                                   3    
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  ILE A  51   N  CYS A  38           
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   ILE A 124                 N   CME A 125     1555   1555  1.33  
LINK         C   CME A 125                 N   TYR A 126     1555   1555  1.33  
LINK         C   THR A 158                 N   CME A 159     1555   1555  1.32  
LINK         C   CME A 159                 N   ASP A 160     1555   1555  1.33  
LINK         C   ILE A 163                 N   CME A 164     1555   1555  1.32  
LINK         C   CME A 164                 N   ASP A 165     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  
CISPEP   1 GLY A   20    PRO A   21          0        -0.48                     
CISPEP   2 GLN A  353    PRO A  354          0         1.04                     
SITE     1 AC1  5 ARG A 189  ARG A 192  TYR A 231  HOH A 633                    
SITE     2 AC1  5 HOH A 671                                                     
SITE     1 AC2  3 HIS A 123  ILE A 254  ARG A 259                               
SITE     1 AC3  5 GLU A 312  GLN A 313  TYR A 314  TYR A 315                    
SITE     2 AC3  5 HOH A 513                                                     
SITE     1 AC4  6 ALA A  50  GLN A 103  ASP A 104  MET A 106                    
SITE     2 AC4  6 HOH A 709  HOH A 617                                          
CRYST1   48.910   70.790   60.410  90.00 108.99  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      0.020446  0.000000  0.007036        0.00000                         
SCALE2      0.000000  0.014126  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017506        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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