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Database: PDB
Entry: 4XRL
LinkDB: 4XRL
Original site: 4XRL 
HEADER    TRANSFERASE                             21-JAN-15   4XRL              
TITLE     CRYSTAL STRUCTURE AT ROOM TEMPERATURE OF ERK2 IN COMPLEX WITH AN      
TITLE    2 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 KINASE INHIBITOR, TRANSFERASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.GELIN,F.ALLEMAND,G.LABESSE,J.F.GUICHOU                              
REVDAT   2   30-MAR-16 4XRL    1       JRNL                                     
REVDAT   1   23-MAR-16 4XRL    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.    2.55 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.4_1496                                    
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) : 2.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.07                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.400                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 88.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 11123                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.162                           
REMARK   3   R VALUE            (WORKING SET) : 0.160                           
REMARK   3   FREE R VALUE                     : 0.229                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.040                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 338                             
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 30.0740 -  3.2176    0.89     5463   172  0.1450 0.1993        
REMARK   3     2  3.2176 -  2.5543    0.88     5322   166  0.1959 0.2988        
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              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.750           
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) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.009           2852                                  
REMARK   3   ANGLE     :  1.214           3866                                  
REMARK   3   CHIRALITY :  0.047            427                                  
REMARK   3   PLANARITY :  0.005            494                                  
REMARK   3   DIHEDRAL  : 15.243           1079                                  
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 4XRL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-MAR-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000206201.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-APR-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007                
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.542                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10787                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.070                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.2                               
REMARK 200  DATA REDUNDANCY                : 1.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.6000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: REFMAC                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MES 100MM PH 6.5, (NH4)2SO4 200MM,       
REMARK 280  BETA-MERCAPTOETHANOL 20MM AND 26% (W/V) PEG MME2000, VAPOR          
REMARK 280  DIFFUSION, SITTING DROP, TEMPERATURE 298K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       35.39300            
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 180 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 16010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -13.0 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 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     TYR A  34    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ASP A 335    CB   CG   OD1  OD2                                  
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  223   CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   NH2  ARG A    89     O    PHE A   346              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    ARG A  13     -104.14     47.82                                   
REMARK 500    GLN A  15      145.79   -175.78                                   
REMARK 500    GLU A  31     -130.66   -105.97                                   
REMARK 500    ALA A  33     -147.31     49.48                                   
REMARK 500    ASP A 147       40.99   -145.88                                   
REMARK 500    ASP A 165       83.48     64.21                                   
REMARK 500    ALA A 184      171.69     71.06                                   
REMARK 500    ALA A 185     -128.70   -151.28                                   
REMARK 500    VAL A 186      -50.60     75.98                                   
REMARK 500    LEU A 198      -58.43   -120.32                                   
REMARK 500    ASN A 199       27.01   -157.83                                   
REMARK 500    GLU A 312      -33.48    -34.68                                   
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 544        DISTANCE =  6.27 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 42A A 402                 
DBREF  4XRL A    9   353  UNP    P63086   MK01_RAT         9    353             
SEQADV 4XRL ALA A  184  UNP  P63086    GLU   184 CONFLICT                       
SEQADV 4XRL ALA A  185  UNP  P63086    TYR   185 CONFLICT                       
SEQRES   1 A  345  PRO GLU MET VAL ARG GLY GLN VAL PHE ASP VAL GLY PRO          
SEQRES   2 A  345  ARG TYR THR ASN LEU SER TYR ILE GLY GLU GLY ALA TYR          
SEQRES   3 A  345  GLY MET VAL CYS SER ALA TYR ASP ASN LEU ASN LYS VAL          
SEQRES   4 A  345  ARG VAL ALA ILE LYS LYS ILE SER PRO PHE GLU HIS GLN          
SEQRES   5 A  345  THR TYR CYS GLN ARG THR LEU ARG GLU ILE LYS ILE LEU          
SEQRES   6 A  345  LEU ARG PHE ARG HIS GLU ASN ILE ILE GLY ILE ASN ASP          
SEQRES   7 A  345  ILE ILE ARG ALA PRO THR ILE GLU GLN MET LYS ASP VAL          
SEQRES   8 A  345  TYR ILE VAL GLN ASP LEU MET GLU THR ASP LEU TYR LYS          
SEQRES   9 A  345  LEU LEU LYS THR GLN HIS LEU SER ASN ASP HIS ILE CYS          
SEQRES  10 A  345  TYR PHE LEU TYR GLN ILE LEU ARG GLY LEU LYS TYR ILE          
SEQRES  11 A  345  HIS SER ALA ASN VAL LEU HIS ARG ASP LEU LYS PRO SER          
SEQRES  12 A  345  ASN LEU LEU LEU ASN THR THR CME ASP LEU LYS ILE CYS          
SEQRES  13 A  345  ASP PHE GLY LEU ALA ARG VAL ALA ASP PRO ASP HIS ASP          
SEQRES  14 A  345  HIS THR GLY PHE LEU THR ALA ALA VAL ALA THR ARG TRP          
SEQRES  15 A  345  TYR ARG ALA PRO GLU ILE MET LEU ASN SER LYS GLY TYR          
SEQRES  16 A  345  THR LYS SER ILE ASP ILE TRP SER VAL GLY CYS ILE LEU          
SEQRES  17 A  345  ALA GLU MET LEU SER ASN ARG PRO ILE PHE PRO GLY LYS          
SEQRES  18 A  345  HIS TYR LEU ASP GLN LEU ASN HIS ILE LEU GLY ILE LEU          
SEQRES  19 A  345  GLY SER PRO SER GLN GLU ASP LEU ASN CYS ILE ILE ASN          
SEQRES  20 A  345  LEU LYS ALA ARG ASN TYR LEU LEU SER LEU PRO HIS LYS          
SEQRES  21 A  345  ASN LYS VAL PRO TRP ASN ARG LEU PHE PRO ASN ALA ASP          
SEQRES  22 A  345  SER LYS ALA LEU ASP LEU LEU ASP LYS MET LEU THR PHE          
SEQRES  23 A  345  ASN PRO HIS LYS ARG ILE GLU VAL GLU GLN ALA LEU ALA          
SEQRES  24 A  345  HIS PRO TYR LEU GLU GLN TYR TYR ASP PRO SER ASP GLU          
SEQRES  25 A  345  PRO ILE ALA GLU ALA PRO PHE LYS PHE ASP MET GLU LEU          
SEQRES  26 A  345  ASP ASP LEU PRO LYS GLU LYS LEU LYS GLU LEU ILE PHE          
SEQRES  27 A  345  GLU GLU THR ALA ARG PHE GLN                                  
MODRES 4XRL CME A  159  CYS  MODIFIED RESIDUE                                   
HET    CME  A 159      10                                                       
HET    SO4  A 401       5                                                       
HET    42A  A 402      11                                                       
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     SO4 SULFATE ION                                                      
HETNAM     42A 1H-PYRROLO[2,3-B]PYRIDINE-3-CARBONITRILE                         
FORMUL   1  CME    C5 H11 N O3 S2                                               
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3  42A    C8 H5 N3                                                     
FORMUL   4  HOH   *44(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 LEU A  232  GLY A  243  1                                  12    
HELIX   10 AB1 SER A  246  CYS 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 ASN A  295  ARG A  299  5                                   5    
HELIX   15 AB6 GLU A  301  ALA A  307  1                                   7    
HELIX   16 AB7 HIS A  308  GLU A  312  5                                   5    
HELIX   17 AB8 ASP A  316  GLU A  320  5                                   5    
HELIX   18 AB9 PRO A  337  ALA A  350  1                                  14    
HELIX   19 AC1 ARG A  351  GLN A  353  5                                   3    
SHEET    1 AA1 2 GLU A  10  MET A  11  0                                        
SHEET    2 AA1 2 VAL A  16  PHE A  17 -1  O  PHE A  17   N  GLU A  10           
SHEET    1 AA2 5 TYR A  23  GLY A  30  0                                        
SHEET    2 AA2 5 VAL A  37  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  GLN A 103   N  ALA A  50           
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  1.32  
LINK         C   CME A 159                 N   ASP A 160     1555   1555  1.33  
CISPEP   1 GLY A   20    PRO A   21          0         0.83                     
CISPEP   2 ALA A  184    ALA A  185          0        -7.12                     
SITE     1 AC1  3 ARG A 189  ARG A 192  TYR A 231                               
SITE     1 AC2  5 ALA A  50  LYS A  52  GLN A 103  ASP A 104                    
SITE     2 AC2  5 MET A 106                                                     
CRYST1   48.479   70.786   60.489  90.00 109.48  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      0.020627  0.000000  0.007296        0.00000                         
SCALE2      0.000000  0.014127  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017536        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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