GenomeNet

Database: PDB
Entry: 3QYZ
LinkDB: 3QYZ
Original site: 3QYZ 
HEADER    TRANSFERASE/TRANSFERASE INHIBITOR       04-MAR-11   3QYZ              
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: MAP KINASE 1, MAPK 1, ERT1, EXTRACELLULAR SIGNAL-REGULATED  
COMPND   5 KINASE 2, ERK-2, MAP KINASE ISOFORM P42, P42-MAPK, MITOGEN-ACTIVATED 
COMPND   6 PROTEIN KINASE 2, MAP KINASE 2, MAPK 2;                              
COMPND   7 EC: 2.7.11.24;                                                       
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: BROWN RAT,RAT,RATS;                                 
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    TRANSFERASE, SERINE/THREONINE-PROTEIN KINASE, ATP-BINDING CELL CYCLE, 
KEYWDS   2 PHOSPHORYLATION, PROTEIN KINASE, TRANSFERASE-TRANSFERASE INHIBITOR   
KEYWDS   3 COMPLEX                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.GELIN,S.POCHET,F.HOH,M.PIROCHI,J.-F.GUICHOU,J.-L.FERRER,G.LABESSE   
REVDAT   3   08-NOV-17 3QYZ    1       REMARK                                   
REVDAT   2   21-MAR-12 3QYZ    1       JRNL                                     
REVDAT   1   24-AUG-11 3QYZ    0                                                
JRNL        AUTH   A.LE MAIRE,M.GELIN,S.POCHET,F.HOH,M.PIROCCHI,J.F.GUICHOU,    
JRNL        AUTH 2 J.L.FERRER,G.LABESSE                                         
JRNL        TITL   IN-PLATE PROTEIN CRYSTALLIZATION, IN SITU LIGAND SOAKING AND 
JRNL        TITL 2 X-RAY DIFFRACTION.                                           
JRNL        REF    ACTA CRYSTALLOGR.,SECT.D      V.  67   747 2011              
JRNL        REFN                   ISSN 0907-4449                               
JRNL        PMID   21904027                                                     
JRNL        DOI    10.1107/S0907444911023249                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.46 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 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) : 1.46                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.17                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.060                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 86.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 62817                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.163                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.195                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.020                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 5599                            
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 46.1893 -  4.5352    0.94     3871   198  0.1782 0.2138        
REMARK   3     2  4.5352 -  3.6002    0.94     3856   211  0.1350 0.1330        
REMARK   3     3  3.6002 -  3.1452    0.93     3831   180  0.1460 0.1791        
REMARK   3     4  3.1452 -  2.8577    0.93     3788   205  0.1609 0.1854        
REMARK   3     5  2.8577 -  2.6529    0.93     3856   215  0.1666 0.2070        
REMARK   3     6  2.6529 -  2.4965    0.92     3713   234  0.1508 0.1747        
REMARK   3     7  2.4965 -  2.3715    0.92     3788   214  0.1510 0.2291        
REMARK   3     8  2.3715 -  2.2682    0.92     3778   225  0.1457 0.2049        
REMARK   3     9  2.2682 -  2.1809    0.93     3832   196  0.1422 0.1589        
REMARK   3    10  2.1809 -  2.1057    0.93     3774   247  0.1387 0.1660        
REMARK   3    11  2.1057 -  2.0398    0.94     3853   214  0.1416 0.1818        
REMARK   3    12  2.0398 -  1.9815    0.94     3896   167  0.1450 0.1730        
REMARK   3    13  1.9815 -  1.9293    0.95     3916   191  0.1408 0.2006        
REMARK   3    14  1.9293 -  1.8823    0.95     3927   182  0.1411 0.1759        
REMARK   3    15  1.8823 -  1.8395    0.96     3971   186  0.1293 0.2043        
REMARK   3    16  1.8395 -  1.8003    0.96     3948   171  0.1373 0.2091        
REMARK   3    17  1.8003 -  1.7643    0.96     4020   202  0.1505 0.1985        
REMARK   3    18  1.7643 -  1.7310    0.95     3798   195  0.1645 0.2067        
REMARK   3    19  1.7310 -  1.7001    0.94     3955   194  0.1679 0.2251        
REMARK   3    20  1.7001 -  1.6713    0.94     3804   204  0.1914 0.2392        
REMARK   3    21  1.6713 -  1.6443    0.89     3715   192  0.1973 0.2380        
REMARK   3    22  1.6443 -  1.6190    0.87     3540   183  0.2132 0.2555        
REMARK   3    23  1.6190 -  1.5952    0.84     3431   204  0.2339 0.2609        
REMARK   3    24  1.5952 -  1.5728    0.79     3231   181  0.2426 0.3180        
REMARK   3    25  1.5728 -  1.5515    0.74     3036   174  0.2817 0.2906        
REMARK   3    26  1.5515 -  1.5313    0.69     2822   137  0.2911 0.3370        
REMARK   3    27  1.5313 -  1.5122    0.63     2631   132  0.3069 0.3355        
REMARK   3    28  1.5122 -  1.4940    0.58     2423   134  0.3370 0.3935        
REMARK   3    29  1.4940 -  1.4766    0.52     2131   114  0.3681 0.3973        
REMARK   3    30  1.4766 -  1.4600    0.46     1884   117  0.4197 0.4303        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.49                                          
REMARK   3   K_SOL              : 0.37                                          
REMARK   3   B_SOL              : 89.75                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.190            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.74860                                             
REMARK   3    B22 (A**2) : 0.85580                                              
REMARK   3    B33 (A**2) : -2.73150                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.22600                                             
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           3089                                  
REMARK   3   ANGLE     :  1.092           4179                                  
REMARK   3   CHIRALITY :  0.074            473                                  
REMARK   3   PLANARITY :  0.006            517                                  
REMARK   3   DIHEDRAL  : 16.074           1214                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 3QYZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-MAR-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000064280.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-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                       : ID14-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : ASYMMETRIC LAUE 001                
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62817                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.460                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 46.170                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
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) : 1.46                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.54                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 73.6                               
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: ISOMORPHOUS REPLACEMENT      
REMARK 200 SOFTWARE USED: ISOMORPHOUS REPLACEMENT                               
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.13                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 26% PEG MME 2000, 0.1M MES, 0.1M         
REMARK 280  AMMONIUM SULFATE, 0.02M BETA-MERCAPTOETHANOL, PH 6.5, VAPOR         
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 291.15K                        
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       35.11850            
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     HIS A    -5                                                      
REMARK 465     HIS A    -4                                                      
REMARK 465     HIS A    -3                                                      
REMARK 465     HIS A    -2                                                      
REMARK 465     HIS A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     ALA A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     GLY A    14                                                      
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     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     GLY A   8    N    CA                                             
REMARK 470     LYS A  97    CG   CD   CE   NZ                                   
REMARK 470     PHE A 329    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LEU A 336    CB   CG   CD1  CD2                                  
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A  351   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    TYR A  34       41.84   -149.29                                   
REMARK 500    ASP A 147       43.38   -149.49                                   
REMARK 500    ASP A 165       83.49     59.89                                   
REMARK 500    ALA A 187      179.24     60.59                                   
REMARK 500    ASN A 199       17.76   -163.56                                   
REMARK 500    LEU A 292       47.41    -96.26                                   
REMARK 500    ASP A 316       93.51   -160.80                                   
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 Z8B A 359                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 360                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 361                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 362                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 363                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 364                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 365                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 366                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 367                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 368                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 369                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS A 370                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 371                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 372                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BME A 373                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3QYU   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3QYW   RELATED DB: PDB                                   
DBREF  3QYZ A    1   358  UNP    P63086   MK01_RAT         1    358             
SEQADV 3QYZ HIS A   -5  UNP  P63086              EXPRESSION TAG                 
SEQADV 3QYZ HIS A   -4  UNP  P63086              EXPRESSION TAG                 
SEQADV 3QYZ HIS A   -3  UNP  P63086              EXPRESSION TAG                 
SEQADV 3QYZ HIS A   -2  UNP  P63086              EXPRESSION TAG                 
SEQADV 3QYZ HIS A   -1  UNP  P63086              EXPRESSION TAG                 
SEQADV 3QYZ HIS A    0  UNP  P63086              EXPRESSION TAG                 
SEQRES   1 A  364  HIS HIS HIS HIS HIS HIS MET ALA ALA ALA ALA ALA ALA          
SEQRES   2 A  364  GLY PRO GLU MET VAL ARG GLY GLN VAL PHE ASP VAL GLY          
SEQRES   3 A  364  PRO ARG TYR THR ASN LEU SER TYR ILE GLY GLU GLY ALA          
SEQRES   4 A  364  TYR GLY MET VAL CYS SER ALA TYR ASP ASN LEU ASN LYS          
SEQRES   5 A  364  VAL ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU HIS          
SEQRES   6 A  364  GLN THR TYR CYS GLN ARG THR LEU ARG GLU ILE LYS ILE          
SEQRES   7 A  364  LEU LEU ARG PHE ARG HIS GLU ASN ILE ILE GLY ILE ASN          
SEQRES   8 A  364  ASP ILE ILE ARG ALA PRO THR ILE GLU GLN MET LYS ASP          
SEQRES   9 A  364  VAL TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU TYR          
SEQRES  10 A  364  LYS LEU LEU LYS THR GLN HIS LEU SER ASN ASP HIS ILE          
SEQRES  11 A  364  CYS TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS TYR          
SEQRES  12 A  364  ILE HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS PRO          
SEQRES  13 A  364  SER ASN LEU LEU LEU ASN THR THR CME ASP LEU LYS ILE          
SEQRES  14 A  364  CYS ASP PHE GLY LEU ALA ARG VAL ALA ASP PRO ASP HIS          
SEQRES  15 A  364  ASP HIS THR GLY PHE LEU THR GLU TYR VAL ALA THR ARG          
SEQRES  16 A  364  TRP TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS GLY          
SEQRES  17 A  364  TYR THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS ILE          
SEQRES  18 A  364  LEU ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO GLY          
SEQRES  19 A  364  LYS HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY ILE          
SEQRES  20 A  364  LEU GLY SER PRO SER GLN GLU ASP LEU ASN CYS ILE ILE          
SEQRES  21 A  364  ASN LEU LYS ALA ARG ASN TYR LEU LEU SER LEU PRO HIS          
SEQRES  22 A  364  LYS ASN LYS VAL PRO TRP ASN ARG LEU PHE PRO ASN ALA          
SEQRES  23 A  364  ASP SER LYS ALA LEU ASP LEU LEU ASP LYS MET LEU THR          
SEQRES  24 A  364  PHE ASN PRO HIS LYS ARG ILE GLU VAL GLU GLN ALA LEU          
SEQRES  25 A  364  ALA HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO SER ASP          
SEQRES  26 A  364  GLU PRO ILE ALA GLU ALA PRO PHE LYS PHE ASP MET GLU          
SEQRES  27 A  364  LEU ASP ASP LEU PRO LYS GLU LYS LEU LYS GLU LEU ILE          
SEQRES  28 A  364  PHE GLU GLU THR ALA ARG PHE GLN PRO GLY TYR ARG SER          
MODRES 3QYZ CME A  159  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
HET    CME  A 159      10                                                       
HET    Z8B  A 359      22                                                       
HET    DMS  A 360       4                                                       
HET    DMS  A 361       4                                                       
HET    DMS  A 362       4                                                       
HET    DMS  A 363       4                                                       
HET    DMS  A 364       4                                                       
HET    DMS  A 365       4                                                       
HET    DMS  A 366       4                                                       
HET    DMS  A 367       4                                                       
HET    DMS  A 368       4                                                       
HET    DMS  A 369       4                                                       
HET    DMS  A 370       4                                                       
HET    SO4  A 371      10                                                       
HET    SO4  A 372       5                                                       
HET    BME  A 373       4                                                       
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     Z8B 5'-AZIDO-8-BROMO-5'-DEOXYADENOSINE                               
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     SO4 SULFATE ION                                                      
HETNAM     BME BETA-MERCAPTOETHANOL                                             
FORMUL   1  CME    C5 H11 N O3 S2                                               
FORMUL   2  Z8B    C10 H11 BR N8 O3                                             
FORMUL   3  DMS    11(C2 H6 O S)                                                
FORMUL  14  SO4    2(O4 S 2-)                                                   
FORMUL  16  BME    C2 H6 O S                                                    
FORMUL  17  HOH   *448(H2 O)                                                    
HELIX    1   1 HIS A   59  PHE A   76  1                                  18    
HELIX    2   2 LEU A  110  GLN A  117  1                                   8    
HELIX    3   3 SER A  120  ALA A  141  1                                  22    
HELIX    4   4 LYS A  149  SER A  151  5                                   3    
HELIX    5   5 ASP A  173  ASP A  177  5                                   5    
HELIX    6   6 THR A  188  ARG A  192  5                                   5    
HELIX    7   7 ALA A  193  ASN A  199  1                                   7    
HELIX    8   8 LYS A  205  ASN A  222  1                                  18    
HELIX    9   9 HIS A  230  LEU A  232  5                                   3    
HELIX   10  10 ASP A  233  GLY A  243  1                                  11    
HELIX   11  11 SER A  246  CYS A  252  1                                   7    
HELIX   12  12 ASN A  255  SER A  264  1                                  10    
HELIX   13  13 PRO A  272  PHE A  277  1                                   6    
HELIX   14  14 ASP A  281  LEU A  292  1                                  12    
HELIX   15  15 GLU A  301  ALA A  307  1                                   7    
HELIX   16  16 HIS A  308  GLU A  312  5                                   5    
HELIX   17  17 ASP A  316  GLU A  320  5                                   5    
HELIX   18  18 PRO A  337  THR A  349  1                                  13    
HELIX   19  19 ALA A  350  GLN A  353  5                                   4    
SHEET    1   A 5 TYR A  23  GLU A  31  0                                        
SHEET    2   A 5 GLY A  35  ASP A  42 -1  O  TYR A  41   N  THR A  24           
SHEET    3   A 5 VAL A  47  ILE A  54 -1  O  VAL A  49   N  ALA A  40           
SHEET    4   A 5 VAL A  99  ASP A 104 -1  O  VAL A  99   N  ILE A  54           
SHEET    5   A 5 ASP A  86  ILE A  88 -1  N  ILE A  88   O  TYR A 100           
SHEET    1   B 3 THR A 108  ASP A 109  0                                        
SHEET    2   B 3 LEU A 153  LEU A 155 -1  O  LEU A 155   N  THR A 108           
SHEET    3   B 3 LEU A 161  ILE A 163 -1  O  LYS A 162   N  LEU A 154           
SHEET    1   C 2 VAL A 143  LEU A 144  0                                        
SHEET    2   C 2 ARG A 170  VAL A 171 -1  O  ARG A 170   N  LEU A 144           
LINK         C   THR A 158                 N   CME A 159     1555   1555  1.34  
LINK         C   CME A 159                 N   ASP A 160     1555   1555  1.33  
CISPEP   1 GLY A   20    PRO A   21          0         1.23                     
CISPEP   2 GLN A  353    PRO A  354          0        -4.00                     
SITE     1 AC1 15 GLY A  30  GLU A  31  GLY A  32  VAL A  37                    
SITE     2 AC1 15 ALA A  50  GLN A 103  ASP A 104  LEU A 105                    
SITE     3 AC1 15 MET A 106  ASP A 109  LYS A 112  LEU A 154                    
SITE     4 AC1 15 DMS A 362  HOH A 563  HOH A 721                               
SITE     1 AC2  7 LYS A 136  HIS A 139  SER A 140  LYS A 205                    
SITE     2 AC2  7 GLU A 303  HOH A 730  HOH A 762                               
SITE     1 AC3  3 THR A 188  TRP A 190  HOH A 627                               
SITE     1 AC4  5 GLY A  32  ALA A  33  TYR A  34  GLY A  35                    
SITE     2 AC4  5 Z8B A 359                                                     
SITE     1 AC5  2 LEU A 114  ASN A 222                                          
SITE     1 AC6  3 ASN A 236  GLY A 240  LYS A 268                               
SITE     1 AC7  5 SER A 221  ARG A 223  PRO A 224  ILE A 225                    
SITE     2 AC7  5 PHE A 277                                                     
SITE     1 AC8  5 ASP A 122  HIS A 123  ILE A 254  ARG A 259                    
SITE     2 AC8  5 TYR A 314                                                     
SITE     1 AC9  6 GLU A  79  ASN A  80  TYR A 126  GLN A 130                    
SITE     2 AC9  6 ARG A 133  HOH A 581                                          
SITE     1 BC1  4 HIS A 297  GLN A 304  HOH A 451  HOH A 589                    
SITE     1 BC2  8 HIS A 118  LEU A 119  LEU A 220  ASN A 279                    
SITE     2 BC2  8 ALA A 280  HOH A 428  HOH A 501  HOH A 624                    
SITE     1 BC3  5 ARG A  77  TYR A 137  ALA A 323  GLU A 324                    
SITE     2 BC3  5 HOH A 775                                                     
SITE     1 BC4  5 TYR A 185  ARG A 189  ARG A 192  TYR A 231                    
SITE     2 BC4  5 HOH A 472                                                     
SITE     1 BC5  4 ARG A  65  ARG A  68  LEU A 168  ARG A 170                    
SITE     1 BC6  2 LEU A 232  TYR A 261                                          
CRYST1   48.689   70.237   59.482  90.00 108.53  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      0.020539  0.000000  0.006884        0.00000                         
SCALE2      0.000000  0.014238  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017731        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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