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Database: PDB
Entry: 6G9N
LinkDB: 6G9N
Original site: 6G9N 
HEADER    SIGNALING PROTEIN                       11-APR-18   6G9N              
TITLE     FRAGMENT-BASED DISCOVERY OF A HIGHLY POTENT, ORALLY BIOAVAILABLE      
TITLE    2 INHIBITOR WHICH MODULATES THE PHOSPHORYLATION AND CATALYTIC ACTIVITY 
TITLE    3 OF ERK1/2                                                            
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: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MAPK1, ERK2, PRKM1, PRKM2;                                     
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    ERK2 KINASE INHIBITOR, SIGNALING PROTEIN                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.O'REILLY                                                            
REVDAT   3   27-JUN-18 6G9N    1       JRNL                                     
REVDAT   2   13-JUN-18 6G9N    1       JRNL                                     
REVDAT   1   30-MAY-18 6G9N    0                                                
JRNL        AUTH   T.D.HEIGHTMAN,V.BERDINI,H.BRAITHWAITE,I.M.BUCK,M.CASSIDY,    
JRNL        AUTH 2 J.CASTRO,A.COURTIN,J.E.H.DAY,C.EAST,L.FAZAL,B.GRAHAM,        
JRNL        AUTH 3 C.M.GRIFFITHS-JONES,J.F.LYONS,V.MARTINS,S.MUENCH,J.M.MUNCK,  
JRNL        AUTH 4 D.NORTON,M.O'REILLY,N.PALMER,P.PATHURI,M.READER,D.C.REES,    
JRNL        AUTH 5 S.J.RICH,C.RICHARDSON,H.SAINI,N.T.THOMPSON,N.G.WALLIS,       
JRNL        AUTH 6 H.WALTON,N.E.WILSHER,A.J.WOOLFORD,M.COOKE,D.COUSIN,S.ONIONS, 
JRNL        AUTH 7 J.SHANNON,J.WATTS,C.W.MURRAY                                 
JRNL        TITL   FRAGMENT-BASED DISCOVERY OF A POTENT, ORALLY BIOAVAILABLE    
JRNL        TITL 2 INHIBITOR THAT MODULATES THE PHOSPHORYLATION AND CATALYTIC   
JRNL        TITL 3 ACTIVITY OF ERK1/2.                                          
JRNL        REF    J. MED. CHEM.                 V.  61  4978 2018              
JRNL        REFN                   ISSN 1520-4804                               
JRNL        PMID   29775310                                                     
JRNL        DOI    10.1021/ACS.JMEDCHEM.8B00421                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.76 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.11.7                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.76                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.25                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 37286                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.168                          
REMARK   3   R VALUE            (WORKING SET)  : 0.165                          
REMARK   3   FREE R VALUE                      : 0.218                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 5.140                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 1918                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 19                       
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 1.76                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 1.81                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 90.61                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 2684                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2227                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 2552                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2212                   
REMARK   3   BIN FREE R VALUE                        : 0.2537                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.92                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 132                      
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2812                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 69                                      
REMARK   3   SOLVENT ATOMS            : 558                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 25.08                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.36                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.32060                                              
REMARK   3    B22 (A**2) : -1.80110                                             
REMARK   3    B33 (A**2) : 0.48050                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.04210                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.210               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.127               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.125               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.158               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.118               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.925                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 5863   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 10619  ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1303   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 74     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 857    ; 16.000 ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 5857   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 382    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 6983   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.013                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.08                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 6.13                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 15.76                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|11 - A|357 }                                       
REMARK   3    ORIGIN FOR THE GROUP (A):   -1.8333    3.5427   38.1537           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0442 T22:   -0.0633                                    
REMARK   3     T33:   -0.0444 T12:    0.0043                                    
REMARK   3     T13:   -0.0187 T23:   -0.0169                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    0.5913 L22:    0.6605                                    
REMARK   3     L33:    0.9627 L12:   -0.1467                                    
REMARK   3     L13:    0.2170 L23:   -0.1090                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0386 S12:   -0.0709 S13:    0.0573                     
REMARK   3     S21:    0.0853 S22:    0.0543 S23:   -0.0804                     
REMARK   3     S31:   -0.0538 S32:    0.0102 S33:   -0.0157                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6G9N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 11-APR-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200009624.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-JAN-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
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 FR-X                        
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 300K               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37533                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.760                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 28.250                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.2                               
REMARK 200  DATA REDUNDANCY                : 2.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 22.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.76                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.81                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 90.4                               
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: FOURIER SYNTHESIS            
REMARK 200 SOFTWARE USED: BUSTER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.55                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M (NH4)2SO4 34% MPEG 2000 .02M          
REMARK 280  MERCAPTOETHANOL .1M PH=7.2 HEPES/NAOH, PH 7.2, VAPOR DIFFUSION,     
REMARK 280  SITTING DROP, TEMPERATURE 293K                                      
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       35.16200            
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 TOTAL BURIED SURFACE AREA: 890 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 16490 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -62.0 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     MET A    -7                                                      
REMARK 465     ALA A    -6                                                      
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     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     GLY A    10                                                      
REMARK 465     PHE A   331                                                      
REMARK 465     ASP A   332                                                      
REMARK 465     TYR A   358                                                      
REMARK 465     ARG A   359                                                      
REMARK 465     SER A   360                                                      
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     LYS A 330    CG   CD   CE   NZ                                   
REMARK 470     ASP A 336    CG   OD1  OD2                                       
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 149       44.02   -153.31                                   
REMARK 500    ASP A 167       85.94     63.57                                   
REMARK 500    ASP A 175       69.27   -151.23                                   
REMARK 500    ALA A 189     -176.26     67.51                                   
REMARK 500    ASN A 201       18.48   -162.65                                   
REMARK 500    LEU A 294       46.29   -101.52                                   
REMARK 500    GLU A 334       66.29     66.62                                   
REMARK 500    PRO A 356      106.50    -47.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY A   85     ILE A   86                  147.08                    
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 A1051        DISTANCE =  5.82 ANGSTROMS                       
REMARK 525    HOH A1052        DISTANCE =  6.17 ANGSTROMS                       
REMARK 525    HOH A1053        DISTANCE =  6.24 ANGSTROMS                       
REMARK 525    HOH A1054        DISTANCE =  6.51 ANGSTROMS                       
REMARK 525    HOH A1055        DISTANCE =  7.01 ANGSTROMS                       
REMARK 525    HOH A1056        DISTANCE =  7.01 ANGSTROMS                       
REMARK 525    HOH A1057        DISTANCE =  8.07 ANGSTROMS                       
REMARK 525    HOH A1058        DISTANCE =  8.62 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 SO4 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ESN A 407                 
DBREF  6G9N A    1   360  UNP    P28482   MK01_HUMAN       1    360             
SEQADV 6G9N MET A   -7  UNP  P28482              INITIATING METHIONINE          
SEQADV 6G9N ALA A   -6  UNP  P28482              EXPRESSION TAG                 
SEQADV 6G9N HIS A   -5  UNP  P28482              EXPRESSION TAG                 
SEQADV 6G9N HIS A   -4  UNP  P28482              EXPRESSION TAG                 
SEQADV 6G9N HIS A   -3  UNP  P28482              EXPRESSION TAG                 
SEQADV 6G9N HIS A   -2  UNP  P28482              EXPRESSION TAG                 
SEQADV 6G9N HIS A   -1  UNP  P28482              EXPRESSION TAG                 
SEQADV 6G9N HIS A    0  UNP  P28482              EXPRESSION TAG                 
SEQRES   1 A  368  MET ALA HIS HIS HIS HIS HIS HIS MET ALA ALA ALA ALA          
SEQRES   2 A  368  ALA ALA GLY ALA GLY PRO GLU MET VAL ARG GLY GLN VAL          
SEQRES   3 A  368  PHE ASP VAL GLY PRO ARG TYR THR ASN LEU SER TYR ILE          
SEQRES   4 A  368  GLY GLU GLY ALA TYR GLY MET VAL CYS SER ALA TYR ASP          
SEQRES   5 A  368  ASN VAL ASN LYS VAL ARG VAL ALA ILE LYS LYS ILE SER          
SEQRES   6 A  368  PRO PHE GLU HIS GLN THR TYR CYS GLN ARG THR LEU ARG          
SEQRES   7 A  368  GLU ILE LYS ILE LEU LEU ARG PHE ARG HIS GLU ASN ILE          
SEQRES   8 A  368  ILE GLY ILE ASN ASP ILE ILE ARG ALA PRO THR ILE GLU          
SEQRES   9 A  368  GLN MET LYS ASP VAL TYR ILE VAL GLN ASP LEU MET GLU          
SEQRES  10 A  368  THR ASP LEU TYR LYS LEU LEU LYS THR GLN HIS LEU SER          
SEQRES  11 A  368  ASN ASP HIS ILE CYS TYR PHE LEU TYR GLN ILE LEU ARG          
SEQRES  12 A  368  GLY LEU LYS TYR ILE HIS SER ALA ASN VAL LEU HIS ARG          
SEQRES  13 A  368  ASP LEU LYS PRO SER ASN LEU LEU LEU ASN THR THR CME          
SEQRES  14 A  368  ASP LEU LYS ILE CYS ASP PHE GLY LEU ALA ARG VAL ALA          
SEQRES  15 A  368  ASP PRO ASP HIS ASP HIS THR GLY PHE LEU THR GLU TYR          
SEQRES  16 A  368  VAL ALA THR ARG TRP TYR ARG ALA PRO GLU ILE MET LEU          
SEQRES  17 A  368  ASN SER LYS GLY TYR THR LYS SER ILE ASP ILE TRP SER          
SEQRES  18 A  368  VAL GLY CYS ILE LEU ALA GLU MET LEU SER ASN ARG PRO          
SEQRES  19 A  368  ILE PHE PRO GLY LYS HIS TYR LEU ASP GLN LEU ASN HIS          
SEQRES  20 A  368  ILE LEU GLY ILE LEU GLY SER PRO SER GLN GLU ASP LEU          
SEQRES  21 A  368  ASN CYS ILE ILE ASN LEU LYS ALA ARG ASN TYR LEU LEU          
SEQRES  22 A  368  SER LEU PRO HIS LYS ASN LYS VAL PRO TRP ASN ARG LEU          
SEQRES  23 A  368  PHE PRO ASN ALA ASP SER LYS ALA LEU ASP LEU LEU ASP          
SEQRES  24 A  368  LYS MET LEU THR PHE ASN PRO HIS LYS ARG ILE GLU VAL          
SEQRES  25 A  368  GLU GLN ALA LEU ALA HIS PRO TYR LEU GLU GLN TYR TYR          
SEQRES  26 A  368  ASP PRO SER ASP GLU PRO ILE ALA GLU ALA PRO PHE LYS          
SEQRES  27 A  368  PHE ASP MET GLU LEU ASP ASP LEU PRO LYS GLU LYS LEU          
SEQRES  28 A  368  LYS GLU LEU ILE PHE GLU GLU THR ALA ARG PHE GLN PRO          
SEQRES  29 A  368  GLY TYR ARG SER                                              
MODRES 6G9N CME A  161  CYS  MODIFIED RESIDUE                                   
HET    CME  A 161      10                                                       
HET    SO4  A 401       5                                                       
HET    SO4  A 402       5                                                       
HET    SO4  A 403       5                                                       
HET    SO4  A 404       5                                                       
HET    SO4  A 405       5                                                       
HET    SO4  A 406       5                                                       
HET    ESN  A 407      71                                                       
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     SO4 SULFATE ION                                                      
HETNAM     ESN (2~{R})-2-[5-[5-CHLORANYL-2-(OXAN-4-YLAMINO)PYRIMIDIN-           
HETNAM   2 ESN  4-YL]-3-OXIDANYLIDENE-1~{H}-ISOINDOL-2-YL]-~{N}-                
HETNAM   3 ESN  [(1~{S})-1-(3-METHYLPHENYL)-2-OXIDANYL-                         
HETNAM   4 ESN  ETHYL]PROPANAMIDE                                               
FORMUL   1  CME    C5 H11 N O3 S2                                               
FORMUL   2  SO4    6(O4 S 2-)                                                   
FORMUL   8  ESN    C29 H32 CL N5 O4                                             
FORMUL   9  HOH   *558(H2 O)                                                    
HELIX    1 AA1 HIS A   61  PHE A   78  1                                  18    
HELIX    2 AA2 LEU A  112  GLN A  119  1                                   8    
HELIX    3 AA3 SER A  122  ALA A  143  1                                  22    
HELIX    4 AA4 LYS A  151  SER A  153  5                                   3    
HELIX    5 AA5 ASP A  175  ASP A  179  5                                   5    
HELIX    6 AA6 THR A  190  ARG A  194  5                                   5    
HELIX    7 AA7 ALA A  195  ASN A  201  1                                   7    
HELIX    8 AA8 LYS A  207  ASN A  224  1                                  18    
HELIX    9 AA9 LEU A  234  GLY A  245  1                                  12    
HELIX   10 AB1 SER A  248  CYS A  254  1                                   7    
HELIX   11 AB2 ASN A  257  LEU A  267  1                                  11    
HELIX   12 AB3 PRO A  274  PHE A  279  1                                   6    
HELIX   13 AB4 ASP A  283  LEU A  294  1                                  12    
HELIX   14 AB5 GLU A  303  ALA A  309  1                                   7    
HELIX   15 AB6 HIS A  310  GLU A  314  5                                   5    
HELIX   16 AB7 ASP A  318  GLU A  322  5                                   5    
HELIX   17 AB8 PRO A  339  ALA A  352  1                                  14    
HELIX   18 AB9 ARG A  353  GLN A  355  5                                   3    
SHEET    1 AA1 2 GLU A  12  VAL A  14  0                                        
SHEET    2 AA1 2 GLN A  17  PHE A  19 -1  O  GLN A  17   N  VAL A  14           
SHEET    1 AA2 5 TYR A  25  GLY A  34  0                                        
SHEET    2 AA2 5 GLY A  37  ASP A  44 -1  O  TYR A  43   N  THR A  26           
SHEET    3 AA2 5 VAL A  49  ILE A  56 -1  O  LYS A  55   N  MET A  38           
SHEET    4 AA2 5 VAL A 101  ASP A 106 -1  O  GLN A 105   N  ALA A  52           
SHEET    5 AA2 5 ASP A  88  ILE A  90 -1  N  ILE A  90   O  TYR A 102           
SHEET    1 AA3 3 THR A 110  ASP A 111  0                                        
SHEET    2 AA3 3 LEU A 155  LEU A 157 -1  O  LEU A 157   N  THR A 110           
SHEET    3 AA3 3 LEU A 163  ILE A 165 -1  O  LYS A 164   N  LEU A 156           
SHEET    1 AA4 2 VAL A 145  LEU A 146  0                                        
SHEET    2 AA4 2 ARG A 172  VAL A 173 -1  O  ARG A 172   N  LEU A 146           
LINK         C   THR A 160                 N   CME A 161     1555   1555  1.33  
LINK         C   CME A 161                 N   ASP A 162     1555   1555  1.35  
CISPEP   1 GLY A   22    PRO A   23          0         0.20                     
SITE     1 AC1  6 ARG A 191  ARG A 194  TYR A 233  HOH A 595                    
SITE     2 AC1  6 HOH A 686  HOH A 738                                          
SITE     1 AC2  6 LYS A 151  SER A 153  THR A 190  HOH A 568                    
SITE     2 AC2  6 HOH A 613  HOH A 711                                          
SITE     1 AC3  2 ARG A 191  HOH A 789                                          
SITE     1 AC4  7 THR A 118  GLN A 119  HIS A 120  ASN A 224                    
SITE     2 AC4  7 HOH A 577  HOH A 619  HOH A 734                               
SITE     1 AC5  7 ASN A 238  HIS A 239  GLY A 242  HOH A 526                    
SITE     2 AC5  7 HOH A 597  HOH A 627  HOH A 645                               
SITE     1 AC6  6 ASP A 283  SER A 284  LYS A 342  HOH A 565                    
SITE     2 AC6  6 HOH A 759  HOH A 783                                          
SITE     1 AC7 19 ILE A  31  TYR A  36  ALA A  52  LYS A  54                    
SITE     2 AC7 19 TYR A  64  ARG A  67  THR A  68  GLN A 105                    
SITE     3 AC7 19 ASP A 106  MET A 108  GLU A 109  THR A 110                    
SITE     4 AC7 19 ASP A 111  LYS A 114  ASP A 167  GLY A 169                    
SITE     5 AC7 19 HOH A 518  HOH A 669  HOH A 850                               
CRYST1   48.904   70.324   60.747  90.00 110.38  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      0.020448  0.000000  0.007597        0.00000                         
SCALE2      0.000000  0.014220  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.017561        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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